Protein inhibitors of serine proteinases

Acta Biochimica Polonica

Volumn 46, Issue 3, 1999, Pages 531-565

  Otlewski, Jacek ^a   Krowarsch, Daniel ^a   Apostoluk, Wlodek ^a  

^a UNIVERSITY OF WROC AW   (Poland)

Author keywords

Canonical conformation; Protein inhibitor; Protein protein recognition; Serine proteinase

Indexed keywords

SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR;

ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; MACROMOLECULE; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; REVIEW;

ANIMALS; BINDING SITES; HUMANS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; SERPINS;

EID: 0033253848     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.1999_4128     Document Type: Review

References (215)

1. Aertgeerts, K., De Bondt, H., De Ranter, C.J. & Declerck, P.J. (1995) Mechanisms contribut́ ing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nature Struct. Biol. 2, 891-897.
2. Antonini, E., Ascenzi, P., Bolognesi, M., Gatti, G., Guarneri, M. & Menegatti, E. (1983) Interaction between (pro)enzyms and Kazal and Kunitz inhibitors. J. Mol. Biol. 165, 543-558.
3. Antuch, W., Berndt, K.D., Chávez, M.A., Delfin, J. & Wüthrich, K. (1993) The NMR solution structure of a Kunitz-type proteinase inhibitor from the sea anemone Stichodactyla helianthus. Eur. J. Biochem. 212, 675-684.
4. Antuch, W., Güntert, P., Billeter, M., Hawthorne, T., Grossenbacher, H. & Wüthrich, K. (1994) NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornthodoros moubata. FEBS Lett. 352, 251-257.
5. Apostoluk, W. & Otlewski, J. (1998) Variability of the canonical loop conformations in serine proteinases inhibitors and other proteins. Proteins: Struct. Funct. Genet. 32, 459-474.
6. Ardelt, W. & Laskowski, M., Jr. (1983). Thermodynamics and kinetics of the hydrolysis and resynthesis of the reactive site peptide bond in turkey ovomucoid third domain by aspergillopeptidase B. Acta Biochim. Polon. 30, 115-126.
7. Ardelt, W. & Laskowski, M., Jr. (1985) Turkey ovomucoid third domain inhibits eight different serine proteinases of varied specificity on the same ... Leu18 - Glu19 ... reactive site. Biochemistry 24, 5313-5320.
8. Ardelt, W. & Laskowski, M., Jr. (1991) Effect of single amino acid replacements on the thermodynamics of the reactive site peptide bond hydrolysis in ovomucoid third domain. J. Mol. Biol. 220, 1041-1053.
9. Ascenzi, P., Amiconi, G., Coletta, M., Lupidi, G., Menegatti, E., Onesti, S. & Bolognesi, M. (1992) Binding of hirudin to α,β and γ-thrombin. A comparative kinetic and thermodynamic study. J. Mol. Biol. 225, 177-184.
10. 1-antichymotrypsin at 2.7 A resolution and its comparison with other serpins. J. Mol. Biol. 218, 595-606.
11. Baumann, U., Bode, W., Huber, R., Travis, J. & Potempa, J. (1991b) Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution. J. Mol. Biol. 226, 1207-1218.
12. 1 substitutions change inhibitory specificity. Eur. J. Biochem. 176, 675-682.
13. Beeser, S.A., Goldenberg, O.P. & Oas, T.G. (1997) Enhanced protein flexibility caused by a destabilizing amino acid replacement in BPTI. J. Mol. Biol. 269, 154-164.
14. Behnke, C.A., Yee, V.C., Trong, I.L., Pedersen, L.C., Stenkamp, R.E., Kim, S.S., Reeck, G.R. & Teller, D.C. (1998) Structural determinants of the bifunctional corn Hageman factor inhibitor: X-ray crystal structure at 1.95 Å resolution. Biochemistry 37, 15277-15288.
15. Berndt, K.D., Güntert, P., Orbons, L.P. & Wüthrich, K. (1992) Determination of a high quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. J. Mol. Biol. 227, 757-775.
16. Betzel, C., Dauter, Z., Genov, N., Lamzin, V., Navaza, J., Schnebli, H.P., Visanji, M. & Wilson, K.P. (1993) Structure of the proteinase inhibitor eglin c with hydrolysed reactive center at 2.0 Å resolution. FEBS Lett. 317,185-188.
17. Björk, I., Ylinenjärvi, K., Olson, S.T. & Bock, P.E. (1992) Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1-P14 region of the putative reactive bond loop of the inhibitor. J. Biol. Chem. 267, 1976-1982.
18. Bode, W. (1979) The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen. J. Mol. Biol. 127, 357-374.
19. Bode, W., Epp, O., Huber, R., Laskowski, M., Jr. & Ardelt, W. (1985) The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3). Eur. J. Biochem. 147, 387-395.
20. Bode, W., Schwager, P. & Huber, R. (1978) The transition of bovine trypsinogen to a trypsinlike state upon ligand binding. The refined crystal structures of bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with the Ile-Val at 1.9 Å resolution. J. Mol. Biol. 118, 99-112.
21. Bode, W., Wei, A.-Z., Huber, R., Meyer, E., Travis, J. & Neuman, S. (1986a) X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of turkey ovomucoid inhibitor. EMBO J. 5, 2453-2458.
22. Bode, W., Papamokos, E., Musil, D., Seemüller, U. & Fritz, H. (1986b) Refined 1.2 Å crystal struc-ture of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. EMBO J. 5, 813-818.
23. Bode, W., Greyling, H.J., Huber, R., Otlewski, J. & Wüusz, T. (1989) The refined 2.0 Å X-ray crystal structure of the complex formed between bovine β-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima): Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes. FEBS Lett. 242, 285-292.
24. Bode, W. & Huber, R. (1992) Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204, 433-451.
25. Bolognesi, M., Gatti, G., Menegatti, E., Guarneri, M., Marquart, M., Papamokos, E. & Huber, R. (1982) Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. J. Mol. Biol. 162, 839-868.
26. Bolognesi, M., Pugliese, L., Gatti, G., Frigero, F., Coda, A., Antolini, L., Schnebli, H.P., Menegatti, E., Amiconi, G. & Ascenzi, P. (1990) X-ray crystal structure of the bovine α-chymotrypsin/eglin c complex at 2.6 Å reso̊ lution. J. Mol. Recogn. 3, 163-168.
27. Bruch, M., Weiss, V. & Engel, J. (1988) Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites. J. Biol. Chem. 263, 16626-16630.
28. Burgering, M.J.M., Orbons, L.P.M., van der Doelen, A., Mulders, J., Theunissen, H.J.M., Grootenhuis, P.D.J., Bode, W., Huber, R. & Stubbs, M.T. (1997) The second Kunitz domain of human tissue factor pathway inhibitor: Cloning, structure determination and interaction with factor Xa. J. Mol. Biol. 269, 395-407.
29. Cai, M., Gong, Y., Kao, J.L.-F. & Krishnamoorthi, R. (1995a) Three-dimensional solution structure of Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy. Biochemistry 34, 5201-5211.
30. Cai, M., Gong, Y., Prakash, O. & Krishnamoorthi, R. (1995b) Reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor-V: Function, thermodynamic stability, and NMR solution structure. Biochemistry 34, 12088-12094.
31. Cai, M., Huang, Y., Prakash, O., Wen, L., Dunkelbarger, S.P., Huang, J.K., Liu, J. & Krishnamoorthi, R. (1996) Differential modulation of binding loop flexibility and stability by Arg50 and Arg52 in Cucurbita maxima trypsin inhibitor-V deduced by trypsin-catalyzed hydrolysis and NMR spectroscopy. Biochemistry 35, 4784-4794.
32. Carrell, R.W., Stein, P.E., Fermi, G. & Wardell, M.R. (1994) Biological implications of a 3 Å structure of dimeric antithrombin. Structure 2, 257-270.
33. Carrell, R., Lomas, D., Stein, P. & Whiststock, J. (1997) Dysfunctional variants and the structural biology of the serpins. Adv. Exp. Med. Biol. 425, 207-222.
34. Castro, M.J.M. & Anderson, S. (1996) Alanine point-mutations in the reactive region of bovine pancreatic trypsin inhibitor: Effects on the kinetics and thermodynamics of binding to β-trypsin and a-chymotrypsin. Biochemistry 35, 11435-11446.
35. Chen, Z. & Bode, W. (1983) Refined 2.5 Å X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor: Crystallisation, Patterson search, structure determination, refinement, structure and comparison with its components and with the bovine trypsin-pancreatic trypsin inhibitor complex. J. Mol. Biol. 164, 283-311.
36. Chen, P., Rose, J., Love, R., Wei, C.H. &Wang, B.C. (1992) Reactive sites of an anticarcino-genic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors. J. Biol. Chem. 267, 1990-1994.
37. Chiche, L., Gaboriaud, C., Heitz, A., Mornon, J.-P., Castro, B. & Kollman, P.A. (1989) Use of restrained molecular dynamics in water to determine three dimensional protein structure: Prediction of the three dimensional structure of Ecballium elaterium trypsin inhibitor II. Proteins: Struct. Funct. Genet. 6, 405-417.
38. Chiche, L., Heitz, A., Padilla, A., Le-Nguyen, D. & Castro, B. (1993) Solution conformation of synthetic bis-headed inhibitor of trypsin and carboxypeptidase A: New structural alignment between the squash inhibitor and the potato carboxypeptidase inhibitor. Protein Engng. 6, 675-682.
39. Czapinska, H. & Otlewski, J. (1999) Structural and energetic determinants of the S1 site specificity in serine proteases. Eur. J. Biochem. 260, 571-595.
40. Dattagupta, J.K., Podder, A., Chakrabarti, C., Sen, U., Mukhopadhyay, D., Dutta, S.K. & Singh, M. (1999) Refined crystal structure (2.3 Å) of a double-headed winged bean alpha-chymotrypsin inhibitor and location of its second reactive site. Proteins 35, 321-331.
41. Dauter, Z., Genov, N., Pipon, N., Wilson, K.S. & Betzel, C. (1991) Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-c. Acta Cryst. B47, 707-730.
42. Delarue, M., Samama, J.-P., Mourey, J.-P. & Moras, D. (1990) Crystal structure of bovine antithrombin III. Acta Crystallog. B46, 550-556.
43. Dennis, M.S. & Lazarus, R.A. (1994a) Kunitz domain inhibitors of tissue factor - factor VIIa: I. Potent inhibitors selected from libraries by phage display. J. Biol. Chem. 269, 22129-22136.
44. Dennis, M.S. & Lazarus, R.A. (1994b) Kunitz domain inhibitors of tissue factor - factor VIIa: II. Potent and specific inhibitors by competitive phage selection. J. Biol. Chem. 269, 22137-22144.
45. Elliott, P.R., Lomas, D.A., Carrell, R.W. & Abrahams, J. P. (1996) Inhibitory conformation of the reactive loop of alpha 1-antitrypsin. Nature Struct. Biol. 3, 676-681.
46. Engh, R., Lobermann, H., Schneider, M., Wiegand, G., Huber, R. & Laurell, C.B. (1989) The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism. Protein Engng. 2, 407-415.
47. Estell, D.A., Wilson, K.A. & Laskowski, M., Jr. (1980) Thermodynamics and kinetics of the hydrolysis of the reactive-site peptide bond in pancreatic trypsin inhibitor (Kunitz) by Dermasterias imbricata trypsin 1. Biochemistry 19, 131-137.
48. Finkenstadt, W.R. & Laskowski, M., Jr. (1967) Resynthesis by trypsin of the cleaved peptide bond in modified soybean trypsin inhibitor. J. Biol Chem. 242, 771-773.
49. Finkenstadt, W.R., Hamid, M.A., Mattis, J.A., Schrode, J.A., Sealock, R.W. & Laskowski, M., Jr. (1974) Kinetics and thermodynamics of the interaction of proteinases with protein inhibitors. Bayer-Symposium V(Fritz, H., Tschesche, H., Greene, L.J. & Truscheit, E. eds.) pp. 389-411, Springer-Verlag, Berlin.
50. Folkers, P.J.M., Clore, G.M., Driscoll, P.C., Dodt, J., Khler, S. & Gronenborn, A.M. (1989) Solution structure of recombinant hirudin and the Lys-47-Glu mutant: A nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. Biochemistry 28, 2601-2617.
51. Francart, C., Dauchez, M., Mix, A.J.P. & Lippens, G. (1997) Solution structure of R-elafin, a specific inhibitor of elastase. J. Mol. Biol. 268, 666-677.
52. Fuentes-Prior, P., Noeske-Jungblut, C., Donner, P., Schleuning, W.-D., Huber, R. & Bode, W. (1997) Structure of thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug. Proc. Natl. Acad. Sci. U.S.A. 94, 11845-11850.
53. Fujinaga, M., Read, R.J., Sielecki, A., Ardelt, W., Laskowski, M., Jr. & James, M.N.G. (1982) Refined crystal structure of the molecular complex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey. Proc. Natl. Acad. Sci. U.S.A. 79, 4868-4872.
54. Fujinaga, M., Sielecki, A.R., Read, R.J., Ardelt, W., Laskowski, M., Jr. & James, M.N.G. (1987) Crystal and molecular structures of the complex of α-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 Å resolution. J. Mol. Biol. 195, 397-418.
55. Gourinath, S., Srinisvasan, A. & Singh, T.P. (1999) Structure of the bifunctional inhibitor of trypsin and α-amylase from ragi seeds at 2.9 Å resolution. Acta Cryst. D55, 25-30.
56. Grasberger, B.L., Clore, G.M. & Gronenborn, A.M. (1994) High-resolution structure of Ascaris trypsin inhibitor in solution: Direct evidence for a pH-induced conformational transition in the reactive site. Structure 2, 669-678.
57. Greenblatt, H.M., Ryan, C.A. & James, M.N.G. (1989) Structure of the complex of Streptomyces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1 Å resolution. J. Mol. Biol. 205, 201-225.
58. Gros, P., Teplyakov, A.V. & Hol, W.G.J. (1992) Effects of eglin-c binding to thermitase: three-dimensional structure comparison of native thermitase and thermitase eglin-c complexes. Proteins: Struct. Funct. Genet. 12, 63-70.
59. Grütter, M.G., Fendrich, G., Huber, R. & Bode, W. (1988) The 2.5 Å X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine a-chymotrypsin. EMBO J. 7, 345-351.
60. Grütter, M.G., Priestle, J.P., Rahuel, J., Gross-enbacher, H., Bode, W., Hofsteenge, J. & Stone, S.R. (1990) Crystal structure of the thrombin-hirudin complex: A novel mode of serine protease inhibition. EMBO J. 9, 2361-2365.
61. 2+ currents from cultured sensory neurones by a novel insect peptide. J. Rcept. Signal. Transduct. Res. 15, 355-364.
62. Harrop, S.J., Jankova, L., Coles, M., Jardine, D., Whittaker, J.S., Gould, A.R., Meister, A., King, G.C., Mabbutt, B.C. & Curmi, P.M.G. (1999) The crystal structure of plasminogen activator inhibitor 2 at 2.0 Å resolution: Implications for serpin function. Structure 7, 43-54.
63. Heald, S.L., Tilton, R.F., Jr., Hammond, L.J., Lee, A., Bayney, R.M., Kamarck, M.E., Ramabhadran, T.V., Dreyer, R.N., Davis, G., Unterbeck, A. & Tambutini, P.P. (1991) Sequential NMR resonance assignment and structure determination of the Kunitz-type inhibitor domain of the Alzheimer's β-amyloid precursor protein. Biochemistry 30, 10467-10478.
64. Hecht, H.J., Szardenings, M., Collins, J. & Schomburg, D. (1991) Three dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type). J. Mol. Biol. 220, 711-722.
65. Hecht, H.J., Szardenings, M., Collins, J. & Schomburg, D. (1992) Three-dimensional structure of a recombinant variant of human pancreatic secretory trypsin inhibitor (Kazal-type). J. Mol. Biol. 225, 1095-1103.
66. Heitz, A., Chiche, L., Le-Nguyen, D. & Castro, B. (1989) 1H 2D NMR and distance geometry study of the folding of Ecbalium elaterium trypsin inhibitor, a member of the squash inhibitor family. Biochemistry 28, 2392-2398.
67. Heinz, D.W., Priestle, J.P., Rahuel, J., Wilson, K.S. & Grütter, M.G. (1991) Refined crystal structures of subtilisin Novo in complex with wild-type and two mutant eglins. J. Mol. Biol. 217, 353-371.
68. Heinz, D.W., Hyberts, S.G., Peng, J.W., Priestle, J.P., Wagner, G. & Grütter, M.G. (1992) Changing the inhibitory specificity and function of the proteinase inhibitor eglin c by site-directed mutagenesis: Functional and structural investigation. Biochemistry 31, 8755-8766.
69. Heiland, R., Leiros, I., Berglund, G.I., Willassen, N.P. & Smalas, A.O. (1998) The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor. Eur. J. Biochem. 256, 317-324.
70. Helland, R., Berglund, G.I., Otlewski, J., Apostoluk, W., Andersen, O.A., Willassen, N.P. & Smalas, A.O. (1999a) High resolution crystal structures of three new trypsin-squash inhibitor complexes. Detailed comparison with other trypsins and their complexes. Acta Cryst. D55, 139-148.
71. Helland, R., Otlewski, J., Sundheim, O., Dadlez, M. & Smalas, A.O. (1999b) The crystal structures of the complexes between bovine β-trypsin and ten P1 variants of BPTI. J. Mol. Biol. 287, 923-942.
72. Hipler, K., Priestle, J.P., Rahuel, J. & Grütter, M. (1992) X-ray crystal structure of the serine proteinase inhibitor eglin c at 1.95 A resolution. FEBS Lett. 309, 139-145.
73. Holak, T.A., Gondol, D., Otlewski, J. & Wilusz, T. (1989) Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamic simulated annealing. J. Mol. Biol. 210, 635-648.
74. Holak, T.A., Habazettl, J., Oschkinat, H. & Otlewski, J. (1991) Structure of proteins in solution derived from homonuclear three-dimensional NOE-NOE nuclear magnetic resonance spectroscopy. High resolution structure of squash trypsin inhibitor. J. Am. Chem. Soc. 113, 3196-3198.
75. 1-Antiproteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways. Biochemistry 33, 8538-8547.
76. Huang, Q., Liu, S. & Tang, Y. (1992) Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family. J. Mol. Biol. 229, 1022-1036.
77. Huang, K., Strynadka, N.C.J., Bernard, V.D. & James, M.N.G. (1994) The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure 2, 669-678.
78. Huang, K., Anderson, S., Laskowski, M., Jr. & James, M.N.G. (1995) Water molecules participate in proteinase-inhibitor interactions: Crystal structures of Leu18, Ala18 and Gly18 variants of turkey ovomucoid inhibitor third domain complexed with Streptomyces griseus proteinase B. Protein Sci. 4, 1985-1997.
79. Huber, R., Kukla, D., Bode, W., Schwager, P., Bartels, K., Deisenhofer, J. & Steigemann, W. (1974) Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. J. Mol. Biol. 89, 73-101.
80. Huber, R., Bode, W., Kukla, D., Kohl, U. & Ryan, C.A. (1975) The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Structure of the anhydro-trypsin-inhibitor complex. Biophys. Struct. Mech. 1, 189-201.
81. Huber, R. & Bode, W. (1978) Structural basis of the activation and action of trypsin. Acc. Chem. Res. 11, 114-122.
82. Hurle, M.R., Marks, C.B., Kosen, P.A., Anderson, S. & Kuntz, I.D. (1990) Denaturant-dependent folding of bovine pancreatic trypsin inhibitor mutants with two-intact disulfide bonds. J. Mol. Biol. 29, 4410-4419.
83. Hyberts, S.G., Goldberg, M.S., Havel, T.F. & Wagner, G. (1992) The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comaprison with X-ray structures. Protein Sci. 1, 736-751.
84. Hynes, T.R., Randal, M., Kennedy, L.A., Eigenbrot, C. & Kossiakoff, A.A. (1990) X-ray crystal structure of the inhibitor domain of Alzheimer's amyloid β-protein precursor. Biochemistry 29, 10018-10022.
85. Janin, J. & Chothia, C. (1990) The structure of protein-protein recognition sites. J. Biol. Chem. 265, 16027-16030.
86. Jin, L., Abrahams, J.P., Skinner, R., Petitou, M., Pike, R.N. & Carrell, R.W. (1997) The anticoagulant activation of antithrombin by heparin. Proc. Natl. Acad. Sci. U.S.A. 94, 14683-14688.
87. Jones, S. & Thornton, J.M. (1996) Principles of protein-protein interactions. Proc. Natl. Acad. Sci. U.S.A. 93, 13-20.
88. Kohfeld, E., Göhring, W., Mayer, U., Zweckstetter, M., Holak, T.A., Chu, M.-L. & Timpl, R. (1996) Conversion of the Kunitz-type module of collagen VI into a highly active trypsin inhibitor by site-directed mutagenesis. Eur. J. Biochem. 238, 333-340.
89. Kojima, S., Nishiyama, Y., Kumagai, I. & Miura, K. (1991) Inhibition of subtilisin BPN′ by reaction site Pl mutants of Streptomyces subtilisin inhibitor. J. Biochem. 109, 377-382.
90. Komiyama, T., Bigler, T.L., Yoshida, N., Noda, K. & Laskowski, M., Jr. (1991) Replacement of P1 Leu18 by Glu18 in the reactive site of turkey ovomucoid third domain converts it into a strong inhibitor of Glu-specific Streptomyces griseus proteinase (GluSGP). J. Biol. Chem. 266, 10727-10730.
91. Komiyama, T., Ray, C.A., Pickup, D.J., Howard, A.D., Thornberry, N.A., Peterson, E.P. & Salvesen, G. (1994) Inhibition of interleukin-1β converting enzyme by the cowpox virus serpin CrmA. J. Biol. Chem. 269, 19331-19337.
92. Krezel, A.M., Darba, P., Robertson, A.D., Fejzo, J., Macura, S. & Markley, J.L. (1994) Solution structure of turkey ovomucoid third domain as determined from nuclear magnetic resonance data. J. Mol. Biol. 242, 203-214.
93. Krokoszynska, I. & Otlewski, J. (1996) Thermodynamic stability effects of single peptide bond hydrolysis in protein inhibitors of serine proteinases. J. Mol Biol. 256, 793-802.
94. Krokoszynska, I., Dadlez, M. & Otlewski, J. (1998) Structure of single-disulfide variants of bovine pancreatic trypsin inhibitor (BPTI) as probed by their binding to bovine β-trypsin. J. Mol. Biol 275, 503-513.
95. 1 variants of bovine pancreatic trypsin inhibitor to four serine proteases. J. Mol. Biol. 289, 175-186.
96. Krystek, S., Stouch, T. & Novotny, J. (1993) Affinity and specificity of serine endopeptidase-protein inhibitor interactions. J. Mol. Biol. 234, 661-679.
97. Lapatto, R., Krengel, U., Schreuder, H.A., Arkema, A., de Boer, B., Kalk, K.H., Hol, W.G.J., Grootenhuis, P.D.J., Mulders, J.W.M., Dijkema, R., Theunissen, H.J.M. & Dijkstra, B.W. (1997) X-ray structure of anistasin at 1.9 A resolution and its modelled complex with blood coagulation factor Xa. EMBO J. 16, 5151-5161.
98. Laskowski, M., Jr. & Sealock, W.R. (1971) Protein proteinase inhibitors-molecular aspects. Enzymes 3, 376-457.
99. Laskowski, M., Jr. & Kato, I. (1980) Protein inhibitors of proteinases. Annu. Rev. Biochem. 49, 593-626.
100. Laskowski, M., Jr. (1986) Protein inhibitors of serine proteinases - mechanism and classification. Adv. Exp. Med. Biol 199, 1-17.
101. Laskowski, M., Jr., Kato, I., Ardelt, W., Cook, J., Denton, A., Empie, M.W., Kohr, W.J., Park, S.J., Parks, K., Schatzley, B.L., Tyashiro, M., Vichot, G., Wheatley, H.E., Wieczorek, A. & Wieczorek, M. (1987) Ovomucoid third domains from 100 avian species: Isolation, sequences, and hypervariability of enzyme-inhibitor contact residues. Biochemistry 26, 202-221.
102. Lawrence, D.A. (1997) The role of reactive-center loop mobility in the serpin inhibitory mechanism. Adv. Exp. Med. Biol. 425, 99-108.
103. Lee, G.F., Lazarus, R.A. & Kelley, R.F. (1997) Potent bifunctional anticoagulants: Kunitz domain-tissue factor fusion proteins. Biochemistry 36, 5609-5611.
104. 1-antitrypsin variant that is as stable as ovalbumin. J. Biol. Chem. 273, 2509-2516.
105. Li, J., Wang, Z., Canagarajah, B., Jiang, H., Kanost, M. & Goldsmith, E.J. (1999) The structure of active serpin 1K from Manduca sexta. Structure 7, 103-109.
106. Li de la Sierra, I., Quillien, L., Flecker, P., Gueguen, J. & Brunie, S. (1999) Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds. J. Mol. Biol. 285, 1195-1207.
107. Liepinsh, E., Berndt, K.D., Sillard, R., Mutt, V. & Otting, G. (1994) Solution structure and dynamics of PEC-60, a protein of the Kazal type inhibitor family, determined by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 239, 137-153.
108. Lim-Wilby, M.S.L., Hallenga, K., de Maeyer, M., Lasters, I., Vlasuk, G.P. & Brunck, T.K. (1995) NMR structure determination of tick anticoagulant peptide (TAP). Protein Sci. 4, 1178-1186.
109. Lin, G., Bode, W., Huber, R., Chi, C. & Engh, R.A. (1993) The 0.25 nm X-ray structure of the Bowman-Birk type inhibitor from mung bean in ternary complex with porcine trypsin. Eur. J. Biochem. 212, 549-555.
110. Liu, J., Praskash, O., Huang, Y., Wen, L., Wen, J.J., Huang, J.-K. & Krishnamoorthi, R. (1996a) Internal mobility of reactive-site-hydrolyzed recombinant Cucurbita maxima trypsin inhibitor-V characterized by NMR spectroscopy: Evidence for differential stabilization of newly formed C- and N-termini. Biochemistry 35, 12503-12510.
111. Liu, J., Prakash, O., Cai, M., Gong, Y., Huang, Y., Wen, L., Wen, J.J., Huang, J.-K. & Krishnamoorthi, R. (1996b) Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy. Biochemistry 35, 1516-1524.
112. 1-antitrypsin. J. Biol. Chem. 270, 5282-5288.
113. 1-proteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177, 531-557.
114. 18 turkey ovomucoid third domain inhibits human furin. J. Biol. Chem. 268, 14583-14585.
115. Lu, W., Qasim, M.A., Laskowski, M., Jr. & Kent, S.B.H. (1997a) Probing intermolecular main chain hydrogen bonding in serine proteinase-protein inhibitor complexes: Chemical synthesis of back-engineered turkey ovomucoid third domain. Biochemistry 36, 673-679.
116. Lu, W., Apostol, I., Qasim, M.A., Warne, N., Wynn, R., Zhang, W.L., Anderson, S., Chiang, Y.W., Ogin, E., Rothberg, I., Ryan, K. & Laskowski, M., Jr. (1997b) Binding of amino acid side chain to S1 cavities of serine proteinases. J. Mol. Biol 266, 441-461.
117. Ludvigsen, S., Shen, H., Kjaer, M., Madsen, J.C. & Poulsen, F.M. (1991) Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals. J. Mol. Biol. 222, 621-635.
118. Lukacs, C.M., Rubin, H. & Christianson, D.W. (1998) Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction. Biochemistry 37, 3297-3304.
119. Makhatadze, G.I., Kim, K.S., Woodward, C. & Privalov, P.L. (1993) Thermodynamics of BPTI folding. Protein Sci. 2, 2028-2036.
120. Markland, W., Ley, A.C. & Ladner, R.C. (1996) Iterative optimization of high affinity protease inhibitors using phage display. 1. Plasmin. Biochemistry 35, 8058-8067.
121. Mathialagan, N. & Hansen, T.R. (1996) Pepsin-inhibitory activity of the uterine serpins. Proc. Natl. Acad. Sci. U.S.A. 93, 13653-13658.
122. McGrath, M.E., Engel, T., Bystroff, C. & Fletterick, R.J. (1994) Macromolecular chelation as an improved mechanism: Structure of the ecotin-trypsin complex. EMBO J. 13, 1502-1507.
123. McGrath, M.E., Gillmor, S.A. & Fletterick, R.J. (1995) Ecotin: Lesson on survival in a protease-filled world. Protein Sci. 4, 141-148.
124. McPhalen, C.A. & James, M.N.G. (1987) Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds. Biochemistry 26, 261-269.
125. McPhalen, C.A. & James, M.N.G. (1988) Structural comparison of two serine proteinase-protein inhibitor complexes: Eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo. Biochemistry 27, 6582-6598.
126. Mer, G., Kellenberger, C., Koehl, P., Stote, R., Sorokine, O., Van Dorsselaer, A.M., Luu, B., Hietter, H. & Lefvére, J.-F. (1994) Solution structure of PMP-D2, a 35-residue peptide isolated from the insect Locusta migratoria. Biochemistry 33, 15397-15407.
127. Mer, G., Hietter, H., Kellenberger, C., Renatus, M., Luu, B. & Lefvre, J.-F. (1996) Solution structure of PMP-C: A new fold in the group of small serine proteinase inhibitors. J. Mol. Biol. 258, 158-171.
128. Merigeau, K., Arnoux, B., Perahia, D., Norris, K. & Ducruix, A. (1998) 1.2 A of the Kunitz-type domain from the 3 chain of human type VI collagen. Acta Cryst. D54, 306-312.
129. Mitsui, Y., Satow, Y. & Sakamaki, T. (1977) Crystal structure of a protein protease inhibitor (Streptomyces subtilisin inhibitor) at 2.3 Å resolution. J. Biochem (Tokyo) 82, 295-298.
130. Mittl, P.R.E., Di Marco, S., Fendrich, G., Pohlig, G., Heim, J., Sommerhoff, C., Fritz, H., Priestle, J.P. & Grütter, M.G. (1996) A new structural class of serine protease inhibitors revealed by the structure of the hirustasinkallikrein complex. Structure 5, 253-264.
131. Morenweiser, R., Auerswald, E.A., van de Locht, A., Fritz, H., Strzebecher, J. & Stubbs, M.T. (1997) Structure-based design of a potent chimeric thrombin inhibitor. J. Biol Chem. 272, 19938-19942.
132. Moses, E. & Hinz, H.-J. (1983) Basic pancreatic trypsin inhibitor has unusual thermodynamic stability parameters. J. Mol. Biol. 170, 765-776.
133. Mottonen, J., Strand, A., Symersky, J., Sweet, R.M., Danley, D.E., Geoghegan, K.F., Gerard, R.D. & Goldsmith, E.J. (1992) Structural basis of latency in plasminogen activator inhibitor-1. Nature 355, 270-273.
134. Mourey, L., Samama, J.-P., Delarue, M., Petitou, M., Choay, J. &Moras, D. (1993) Crystal structure of cleaved bovine antithrombin III at 3.2 A resolution. J. Mol. Biol. 232, 223-241.
135. Mühlhahn, P., Czisch, M., Morenweiser, R., Habermann, B., Engh, R.A., Sommerhoff, C.P., Auerswald, E.A. & Holak, T.A. (1994) Structure of leech derived tryptase inhibitor (LDTI-C) in solution. FEBS Lett. 355, 290-296.
136. Musil, D., Bode, W., Huber, R., Laskowski, M., Jr., Lin, T.-Y. & Ardelt, W. (1991) Refined X-ray crystal structures of the reactive site modified ovomucoid inhibitor third domains from silver pheasant (OMSVP3*) and from Japanese quail (OMJPQ3*). J. Mol. Biol. 220, 739-755.
137. Nielsen, K.J., Alewood, D., Andrews, J., Kent, S.B.H. & Craik, D.J. (1994a) An 1H NMR determination of the three dimensional structures of mirror image forms of a Leu-5 variant of the trypsin inhibitor from Ecbalium elaterium (EETI II). Protein Sci. 3, 291-302.
138. Nielsen, K.J., Heath, R.L., Anderson, M.A. & Craik, D.J. (1994b) The three dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata. J. Mol. Biol. 242, 231-243.
139. Nielsen, K.J., Heath, R.L., Anderson, M.A. & Craik, D.J. (1995) Structures of a series of 6-kDa trypsin inhibitors isolated from the stigma of Nicotiana alata. Biochemistry 34, 14304-14311.
140. Neurath, H. (1984) Evolution of proteolytic enzymes. Science 224, 350-357.
141. Onesti, S., Brick, P. & Blow, D.M. (1991) Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina coffra, seeds. J. Mol. Biol. 217, 153-176.
142. Osmark, P., Sorensen, P. & Poulsen, F.M. (1993) Context dependent of protein secondary structure formation: The three-dimensional structure and stability of a hybrid between chymotrypsin inhibitor 2 and helix E from subtilisin Carlsberg. Biochemistry 32, 11007-11014.
143. Otlewski, J. & Zbyryt, T. (1994) Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. I. Kinetics and thermodynamics of the interaction between squash inhibitors and bovine β-trypsin. Biochemistry 33, 200-207.
144. Otlewski, J., Zbyryt, T., Dryjanski, M., Bulaj, G. & Wilusz, T. (1994) Single peptide bond hydrolysis/resynthesis in squash inhibitors of serine proteinases. II. Limited proteolysis of Cucurbita maxima trypsin inhibitor I (CMTI I) by pepsin. Biochemistry 33, 208-213.
145. Pal, G.P., Kavounis, C.A., Jany, K.D. & Tsernoglou, D. (1994) The
146. Peng, J.W. & Wagner, G. (1992) Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments. Biochemistry 31, 8571-8586.
147. Pereira, P.J., Bergner, A., Macedo-Riberio, S., Huber, R., Matschiaer, G., Fritz, H., Sommerhoff, C.P. & Bode, W. (1998) Human beta-tryptase is aring-like treatment with active sites facing a central pore. Nature 392, 306-311.
148. Perona, J.J., Tsu, C.A., Fletterick, R.J. & Craik, C.S. (1993) Crystal structures of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI. J. Mol. Biol. 230, 919-933.
149. Perona, J.J., Tsu, C.A., Craik, C.S. & Fletterick, R.J. (1997) Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix. Biochemistry 36, 5381-5392.
150. Polanowska, J., Krokoszynska, I., Czapinska, H., Watorek, W., Dadlez, M. & Otlewski, J. (1998) Specificity of human cathepsin G. Biochim. Biophys. Acta 1386, 189-198.
151. Potempa, J., Korzus, E. & Travis, J. (1994) The serpin superfamily of proteinase inhibitors: structure, function, and regulation. J. Biol. Chem. 269, 15957-15960.
152. Priestle, J.P. & Di Marco, S. (1997) Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LD-TI-tryptase system. Structure 5, 1465-1474.
153. Qasim, M.A., Ranjbar, M.R., Wynn, R., Anderson, S. & Laskowski, M., Jr. (1995) Ionizable P1 residues in serine proteinase inhibitors undergo large pK shifts on complex formation. J. Biol. Chem. 270, 1-4.
154. 1 variants of eglin c and of turkey ovomucoid third domain with serine proteinases. Biochemistry 36, 1598-1607.
155. Quast, U., Engel, J., Steffen, E., Tschesche, H. & Kupfer, S. (1978) Kinetics of the interaction of a-chymotrypsin with trypsin kallikrein inhibitor (Kunitz) in which the reactive-site peptide bond Lys-15-Ala16 is split. Eur. J. Biochem. 86, 353-360.
156. Read, R.J., Fujinaga, M., Sielecki, A.R. & James, M.N.G. (1983) Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8 Å resolution. Biochemistry 22, 4420-4433.
157. Roberts, B.L., Markland, W., Ley, A.C., Kent, R.B., White, D.W., Guterman, S.K. & Ladner, R.C. (1992) Directed evolution of a protein: Selection of potent neutrophil elastase inhibitors displayed on M13 fusion phages. Proc. Natl. Acad. Sci. U.S.A. 89, 2429-2433.
158. Rydel, T.J., Ravichandran, K.G., Tulinsky, A., Bode, W., Huber, R., Roitsch, C. & Fenton, J.W. (1990) The structure of a complex of recombinant hirudin and human β-thrombin, Science 249, 277-280.
159. Rydel, T.J., Tulinsky, A., Bode, W. & Huber, R. (1991) Refined structure of the hirudin-thrombin complex. J. Mol. Biol. 221, 583-601.
160. 1-antitrypsin at 2.7 Å. Structure 4, 1181-1192.
161. Schechter, I. & Berger, A. (1967) On the size of the active site in proteases. Biochem. Biophys. Res. Commun. 27, 157-162.
162. Scheidig, A.J., Hynes, T.R., Pelletier, L.A., Wells, J.A. & Kossiakoff, A.A. (1997) Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid β-precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): Engineering of inhibitors with altered specificities. Protein Sci. 6, 1806-1824.
163. Schreuder, H.A., de Boer, B., Dijkema, R., Mulders, J., Theunissen, H.J.M., Grootenhuis, P.D.J. & Hol, W.G.J. (1994) The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions. Nature Struct. Biol. 1, 48-54.
164. Schulze, A.J., Baumann, U., Knof, S., Jaeger, E., Huber, R. & Laurell, C.B. (1990) Structural transition of alpha 1-antitrypsin by a peptide sequentially similar to beta-strand s4A. Eur. J. Biochem. 194, 51-56.
165. Seeram, S.S., Hiraga, K. & Oda, K. (1997) Peptide bond and temporary inhibition of Streptomyces metalloproteinase inhibitor. J. Biochem. (Tokyo) 122, 788-794.
166. Sharp, A.M., Stein, P.E., Pannu, N.S., Carrell, R.W., Berkenpas, M.B., Ginsburg, D., Lawrence, D.A. & Read, R.J. (1999) The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Structure 7, 111-118.
167. Shaw, G.L., Davis, B., Keeler, J. & Fersht, A.R. (1995) Backbone dynamics of chymotrypsin inhibitor 2: Effect of breaking the active site bond and its implications for the mechanism of inhibition of serine proteases. Biochemistry 34, 2225-2233.
168. Shin, D.H., Song, H.K., Seong, I.S., Lee, C.S., Chung, C.H. & Suh, S.W. (1996) Crystal structure analyses of uncomplexed ecotin in two crystal forms: Implications for its function and stability. Protein Sci. 5, 2236-2247.
169. Shore, J.D., Day, D.E., Francis-Chmura, A.M., Verhamme, I., Kvasman, J., Lawrence, D.A. & Ginsburg, D. (1995) A fluorescent probe of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism. J. Biol. Chem. 270, 5395-5398.
170. 16 reactive-site peptide bond in bovine pancreatic trypsin inhibitor (aprotinin). J. Prot. Chem. 7, 633-640.
171. Skinner, R., Abrahams, J.-P., Whisstock, J.C., Lesk, A.M., Carrell, R-W. & Wardell, M.R. (1997) The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site. J. Mol. Biol. 266, 601-609.
172. Skinner, R., Chang, W.S.W., Jin, L., Pei, X., Huntington, J.A., Abrahams, J.P., Carrell, R.W. & Lomas, D.A. (1998) Implications for function and therapy of a 2.9 Å structure of binary-complexed antithrombin. J. Mol. Biol. 283, 9-14.
173. Song, H.K. & Suh, S.W. (1998) Kunitz-type soybean trypsin inhibitor revisited: Refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator. J. Mol. Biol. 275, 347-363.
174. Stein, P.E., Tewkesbury, C. & Carrell, R.W. (1989) Ovalbumin and angiotensinogen lack serpin S-R conformational change. Biochem. J. 262, 103-107.
175. Stein, P., Leslie, A.G.W., Finch, J.T., Turnell, W.G., McLaughlin, P.J. & Carrell, R.W. (1990) Crystal structure of ovalbumin as a model for the reactive center of serpins. Nature 347, 99-102.
176. Stein, P., Leslie, A.G.W., Finch, J.T. & Carrell, R.W. (1991) Crystal structure of uncleaved ovalbumin at 1.95 Å resolution. J. Mol. Biol. 221, 941-959.
177. Stein, P.E. & Carrell, R.W. (1995) What do dysfunctional serpins tell us about molecular mobility and disease? Nature Struct. Biol. 2, 96-113.
178. Stone, S.R., Whisstock, J.C., Bottomely, S.P. & Hopkins, P.C.R. (1997) Serpins. A mechanistic class of their own. Adv. Exp. Med. Biol. 425, 5-15.
179. Strobl, S., Mühlhahn, P., Bernstein, R., Wiltscheck, R., Maskos, K., Wunderlich, M., Huber, R., Glockshuber, R. & Holak, T.A. (1995) Determination of the three-dimensional structure of the bifunctional α-amylase/ trypsin inhibitor from ragi seeds by NMR spectroscopy. Biochemistry 34, 8281-8293.
180. Strobl, S., Maskos, K., Wiegand, G., Huber, R., Gomis-Rüth, F.X. & Glockshuber, R. (1998) A novel strategy for inhibition of α-amylases: Yellow meal worm α-amylase in complex with the ragi bifunctional inhibitor at 2.5 Å resolution. Structure 6, 911-921.
181. Stubbs, M.T. & Bode, W. (1995) The clot thickens: Clues provided by thrombin structure. Trends Biochem. Sci. 20, 23-28.
182. Stubbs, M.T., Morenweiser, R., Stürzebecher, J., Bauer, M., Bode, W., Huber, R., Piechottka, G.P., Matschiner, G., Sommerhoff, C.P., Fritz, H. & Auerswald, E.A. (1997) The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. J. Biol. Chem. 272, 19931-19937.
183. Suzuki, A., Yamane, T., Ashida, T., Norioka, S., Hara, S. & Ikenaka, T. (1993) Crystallographic refinement of Bowman-Birk type proteases inhibitor A-II from peanut (Arachis hypogaea) at 2.3 Å resolution. J. Mol. Biol. 234, 722-734.
184. Szyperski, T., Güntert, P., Stone, S.R. & Wüthrich, K. (1992a) Nuclear magnetic resonance solution structure of hirudin(1-51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain. J. Mol. Biol. 228, 1193-1205.
185. Szyperski, T., Güntert, P., Stone, S.R., Tulinsky, A., Bode, W., Huber, R. & Wüthrich, K. (1992b) Impact of protein-protein contacts on the conformation of thrombin-bound hirudin studied by comparison with the nuclear magnetic resonance solution structure of hirudin (1-51). J. Mol. Biol. 228, 1206-1211.
186. Takeuchi, Y., Satow, Y., Nakamura, K.T. & Mitsui, Y. (1991) Refined crystal structure of the complex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution. J. Mol. Biol. 221, 309-325.
187. Takeuchi, Y., Nonaka, T., Nakamura, K.T., Kojima, S., Miura, K.-I. & Mitsui, Y. (1992) Crystal structure of an engineered subtilisin inhibitor complexed with bovine trypsin. Proc. Natl. Acad. Sci. U.S.A. 89, 4407-4411.
188. Tamura, A., Kanaori, K., Kojima, S., Kumagai, I., Miura, K. & Akasaka, K. (1991) Mechanism of temporary inhibition in Streptomyces subtilisin inhibitor induced by an amino acid substitution, tryptophan 86 replaced by histidine. Biochemistry 30, 5275-5286.
189. Travis, J. & Salvesen, G.S. (1983) Human plasma proteinase inhibitors. Annu. Rev. Biochem. 52, 655-709.
190. Tsunemi, M., Matsuura, Y., Sakakibara, S. & Katsube, Y. (1996) Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 Å resolution. Biochemistry 35, 11570-11576.
191. Tsunogae, Y., Tanaka, I., Yamane, T., Kikkawa, J., Achida, J.T., Ishikawa, C., Watanabe, K., Nakamura, S. & Takahashi, K. (1986) Structure of the trypsin-binding domain of Bowman-Birk type protease inhibitor and its interaction with trypsin. J. Biochem (Tokyo) 100, 1637-1646.
192. Tucker, H.M., Mottonen, J., Goldsmith, E.J. & Gerard, R.D. (1995) Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition. Nature Struct. Biol. 2, 442-445.
193. Uson, I., Sheldrick, G.M., de La Fortelle, E., Bricogne, G., Di Marco, S., Priestle, J.P. & Grutter, M.G. (1999) The 1.2 Å crystal structure of hirustasin reveals the intrinsic flexibility of a family of highly disulphide-bridged serine proteases. Structure 7, 55-63.
194. Vallee, F., Kadziola, A., Bourne, Y., Juy, M., Rodenburg, K.W., Svensson, B. & Haser, R. (1998) Barley α-amylase bound to its endogenous protein inhibitor BASI: Crystal structure of the complex at 1.9 Å resolution. Structure 6, 649-659.
195. van de Locht, A., Lamba, D., Bauer, M., Huber, R., Friedrich, T., Kroger, B., Hoffken, W. & Bode, W. (1995) Two heads are better than one: Crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J. 14, 5149-5157.
196. van de Locht, A., Stubbs, M.T., Bode, W., Friedrich, T., Bollschweiler, C., Hoffken, W. & Huber, R. (1996) The ornithodorin-thrombin crystal structure, a key to the TAP enigma? EMBO J. 22, 6011-6017.
197. van de Locht, A., Bode, W., Huber, R., Le Bonniec, B.F., Stone, S.R., Esmon, C.T. & Stubbs, M.T. (1997) The thrombin E192Q-BPTI complex reveals gross structural rearrangements for the interaction with antithrombin and thrombo-modulin. EMBO J. 16, 2977-2984.
198. Walkenhorst, W.F., Krezel, A.M., Rhyu, G.I. & Markley, J.L. (1994) Solution structure of reactive site hydrolyzed turkey ovomucoid third domain by nuclear magnetic resonance and distance geometry methods. J. Mol. Biol. 242, 215-230.
199. Wardell, M.R., Abrahams, J.P., Bruce, D., Skinner, R. & Leslie, A.G. (1993) Crystallization and preliminary X-ray diffraction analysis of two conformations of intact human anti-thrombin. J. Mol. Biol. 234, 1253-1258.
200. Waxman, L., Smith, D.E., Arcuri, K.E. & Vlasuk, G.P. (1990) Tick anticoagulant peptide (tap) is a novel inhibitor of blood coagulation factor Xa. Science 248, 593-596.
201. Wei, A., Rubin, H., Cooperman, B.S. & Christianson, D.W. (1994) Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Nature Struct. Biol. 1, 251-257.
202. Wei, A., Alexander, R.S., Duke, J., Ross, H., Rosenfeld, S.A. & Chang, C.H. (1998) Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa. J. Mol. Biol. 283, 147-154.
203. Wells, J.A. (1990) Additivity of mutational effects in proteins. Biochemistry 29, 8509-8517.
204. Werner, M.H. & Wemmer, D.E. (1992) Three-dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution. Biochemistry 31, 999-1010.
205. Whisstock, J., Skinner, R. & Lesk, A.M. (1998) An atlas of serpin conformations. Trends Biochem. Sci. 23, 63-67.
206. Wlodawer, A., Walter, J., Huber, R. & Sjolin, L. (1984) Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and X-ray refinement of crystal form II. J. Mol. Biol. 180, 301-329.
207. Wright, H.T. & Scarsdale, J.N. (1995) Structural basis for serpin inhibitor activity. Proteins: Struct. Funct. Genet. 22, 210-225.
208. Wright, H.T., Qian, H.Z. & Huber, R. (1990) Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin. J. Mol. Biol. 213, 513-528.
209. Xu, Y., Carr, P.D., Guss, J.M. & Ollis, D.L. (1998) The crystal structure of bikunin from the inter α-inhibitor complex: A serine protease inhibitor with two Kunitz domains. J. Mol. Biol. 276, 955-966.
210. Yang, S.Q., Wang, C.-I., Gillmor, S.A., Fletterick, R.J. & Craik, C.S. (1998) Ecotin: A serine protease inhibitor with two distinct and interact ing binding sites. J. Mol. Biol. 279, 945-957.
211. Yu, M.-H., Weissman, J.S. & Kim, P.S. (1995) Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. J. Mol. Biol. 249, 388-397.
212. Zbyryt, T. & Otlewski, J. (1991) Interaction between squash inhibitors and bovine trypsinogen. Biol. Chem. Hoppe-Seyler 372, 255-262.
213. Zemke, K.J., Müller-Farhnow, A., Jany, K.-D., Pal, G.P. & Saenger, W. (1991) The three-dimensional structure of the bifunctional proteinase K/α-amylase inhibitor from wheat (PKI3) at 2.5 Å resolution. FEBS Lett. 279, 240-242.
214. a inhibited with a BPTI mutant. J. Mol. Biol. 285, 2089-2104.
215. Zweckstetter, M., Czisch, M., Mayer, U., Chu, M.-L., Zinth, W., Timpl, R. & Holak, T.A. (1995) Structure and multiple conformations of the Kunitz-type domain from human type VI collagen α3(VI) chain in solution. Structure 4, 195-209.