The crystal structure of plasminogen activator inhibitor 2 at 2.0 Å resolution: Implications for serpin function

Structure

Volumn 7, Issue 1, 1999, Pages 43-54

  Harrop, Stephen J ^a   Jankova, Lucy ^a   Coles, Murray ^b   Jardine, Daniel ^b   Whittaker, Jason S ^a   Gould, Alison R ^c   Meister, Andreas ^c   King, Garry C ^a   Mabbutt, Bridget C ^b   Curmi, Paul MG ^a  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

^b MACQUARIE UNIVERSITY   (Australia)

^c Biotechnology Australia   (Australia)

Author keywords

PAI 2; Pair correlations; Reactive centre loop; Serpin; Urokinase

Indexed keywords

ALPHA 1 ANTITRYPSIN; CHYMOTRYPSIN INHIBITOR; COMPLEMENT COMPONENT C1S INHIBITOR; HEAT SHOCK PROTEIN 47; MASPIN; OVALBUMIN; PLASMINOGEN ACTIVATOR INHIBITOR; SERINE PROTEINASE INHIBITOR; THYROXINE BINDING PROTEIN; UNCLASSIFIED DRUG; UTEROFERRIN;

ARTICLE; CRYSTAL STRUCTURE; HUMAN; HUMAN CELL; HYDROGEN BOND; MOLECULAR INTERACTION; PLASMINOGEN ACTIVATION; PRIORITY JOURNAL; PROTEINASE INHIBITION; STATISTICAL ANALYSIS; STRUCTURE ANALYSIS;

EID: 0033555456     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80008-2     Document Type: Article

References (54)

1. Kruithof, E.K.O., Baker, M.S. & Bunn, C.L. (1995). Biological and clinical aspects of plasminogen activator inhibitor type 2. Blood 86, 4007-4024.
2. Gettins, P.G.W., Patston, P.A. & Olson, S.T. (1996). Serpins: Structure, Function and Biology. Springer, New York, USA.
3. 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.
4. Stein, P.E., 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 centre loop of serpins. Nature 347, 99-102.
5. 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. Nat. Struct. Biol. 1, 251-257.
6. Schlechter, I. & Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
7. Jensen, P.H., et al., & Rasmussen, L.K. (1994). A unique interhelical insertion in plasminogen activator inhibitor-2 contains three glutamines, Gln83, Gln84, Gln86, essential for transglutaminase-mediated cross-linking. J. Biol. Chem. 269, 15394-15398.
8. Stein, P.E., 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.
9. Baumann, U., Bode, W., Huber, R., Travis, J. & Potempa, J. (1992). Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 Å resolution. J. Mol. Biol. 226, 1207-1218.
10. Remold-O'Donnell, E. (1993). The ovalbumin family of serpin proteins. FEBS Lett. 315, 105-108.
11. 1-antitrypsin. Nat. Struct. Biol. 3, 676-681.
12. Laskowski, M. & Kato, I. (1980). Protein inhibitors of proteinases. Annu. Rev. Biochem. 49, 593-626.
13. Bode, W. & Huber, R. (1992). Natural protein proteinase inhibitors and their interactions with proteinases. Eur. J. Biochem. 204, 433-451.
14. 1-proteinase inhibitor. Biochemistry 30, 9054-9060.
15. 1-proteinase inhibitor probed by limited proteolysis. Biochemistry 31, 2720-2728.
16. Chang, W.-S.W., Wardell, M.R., Lomas, D.A. & Carrell, R.W. (1996). Probing serpin reactive-loop conformations by proteolytic cleavage. Biochem. J. 314, 647-653.
17. 1-antitrypsin for structure and function of serpins. Biochemistry 28, 8951-8966.
18. 1-antitrypsin Piz. FEBS Lett. 65, 195-197.
19. Stein, P.E. & Carrell, R.W. (1995). What do dysfunctional serpins tell us about molecular mobility and disease? Nat. Struct. Biol. 2, 96-113.
20. Schreuder, H.A., et al., & Hol, W.G.J. (1994). The intact and cleaved human antithrombin III complex as a model for serpin-protease interactions. Nat. Struct. Biol. 1, 48-54.
21. Wouters, M.A. & Curmi, P.M.G. (1995). An analysis of side chain interaction and pair correlations within antiparallel β-sheets: The difference between backbone hydrogen-bonded and non-hydrogen bonded residue pairs. Proteins 22, 119-131.
22. Smith, C.K. & Regan, L. (1995). Guidelines for protein design: The energetics of β-sheet sidechain interactions. Science 270, 980-982.
23. Cootes, A.P., Curmi, P.M.G., Cunningham, R., Donnelly, C. & Torda, A.E. (1998). The dependence of amino acid pair correlations on structural environment. Proteins 32, 175-189.
24. 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.
25. Hopkins, P.C.R., Chang, W.-S., Wardell, M.R. & Stone, S.R. (1997). Inhibitory mechanism of serpins. Mobility of the C-terminal region of the reactive-site loop. J. Biol. Chem. 272, 3905-3909.
26. Wilczynska, M., Fa, M., Ohlsson, P.-I. & Ny, T. (1995). The inhibition mechanism of serpins. J. Biol. Chem. 270, 29652-29655.
27. Lawrence, D.A., et al., & Shore, J.D. (1995). Serpin-protease complexes are trapped as stable acyl-enzyme intermediates. J. Biol. Chem. 270, 25309-25312.
28. Olson, S.T., et al., & Bjork, I. (1995). Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. J. Biol. Chem. 270, 30007-30017.
29. Engh, R.A., Huber, R., Bode, W. & Schulze, A.J. (1995). Divining the serpin inhibition mechanism: A suicide substrate "springe"? Trends Biochem. Sci. 13, 503-510.
30. 1-antitrypsin (358Met→Arg)-trypsin, antitrypsin-elastase. Proteins 26, 288-303.
31. 1-antitrypsin to its reaction with elastase. Biochemistry 34, 15872-15879.
32. 1-proteinase inhibitor variants. Eur. J. Biochem. 202, 1147-1155.
33. 1-proteinase inhibitor in Escherichia coli: Effects of single amino acid substitutions in the active site loop on aggregate formation. J. Biotechnol. 32, 231-238.
34. Audenaert, A.-M., Knockaert, I., Collen, D. & Declerck, P.J. (1994). Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop. J. Biol. Chem. 269, 19559-19564.
35. 1-antitrypsin by a peptide sequentially similar to β-strand s4A. Eur. J. Biochem. 194, 51-56.
36. 1 proteinase inhibitor in β-sheet A. Biochemistry 31, 7560-7565.
37. Saunders, D.N., Buttigieg, K.M.L., Gould, A., McPhun, V. & Baker, M.S. (1998). Immunological detection of conformational neoepitopes associated with the serpin activity of plasminogen activator inhibitor type-2. J. Biol. Chem. 273, 10965-10971.
38. Xue, Y., et al., & Deinum, J. (1998). Interfering with the inhibitory mechanism of serpins: Crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide. Structure 6, 627-636.
39. Wilczynska, M., Fa, M., Karolin, J., Ohlsson, P.-I., Johansson, L.B.-Å. & Ny, T. (1997). Structural insights into serpin-protease complexes reveal the inhibitory mechanism of serpins. Nat. Struct. Biol. 4, 354-357.
40. Stratikos, E. & Gettins, P.G.W. (1997). Major proteinase movement upon stable serpin-proteinase complex formation. Proc. Natl Acad. Sci. USA 94, 453-458.
41. Wright, H.T. (1996). The structural puzzle of how serpin serine protease inhibitors work. BioEssays 18, 453-464.
42. Wright, H.T. & Scarsdale, J.N. (1995). Structural basis for serpin inhibitor activity. Proteins 22, 210-225.
43. Plotnick, M.I., Mayne, L, Schechter, N.M. & Rubin, H. (1996). Distortion of the active site of chymotrypsin complexed with a serpin. Biochemistry 35, 7586-7590.
44. Otwinowski, Z. & Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
45. Brünger, A.T. (1992). X-PLOR 3.1 A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
46. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991 ). Improved methods for building protein models in electron density maps and correction of errors in these models. Acta Cryst. A 47, 110-119.
47. Brünger, A.T. (1992). Free R-value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
48. Collaborative Computing Project, No. 4. (1994). The CCP4 suite: Programs for protein crystallography. Acta Cryst. D 50, 760-763.
49. Murshudov, G.N., Vagin, A.A. & Dodson, E.J. (1997). Refinement of macromolecular structures by the maximum likelihood method. Acta Cryst. D 53, 240-255.
50. Sander, C. & Schneider, R. (1991). Database of homology-derived protein structures. Proteins 9, 56-68.
51. Hobohm, U., Scharf, M., Schneider, R. & Sander, C. (1992). Selection of representative protein data sets. Protein Sci. 1, 409-417.
52. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1994). PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
53. Kraulis, P.J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst 24, 946-950.
54. Evans, S.V. (1993). SETOR: Hardware enlightened three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11, 134-138.