메뉴 건너뛰기




Volumn 268, Issue 3, 1997, Pages 666-677

Solution structure of R-elafin, a specific inhibitor of elastase

Author keywords

Binding loop; Disulfide bridges; Elastase inhibitor; NMR; SLPI

Indexed keywords

APROTININ; ELAFIN; ELASTASE INHIBITOR; PROTEINASE INHIBITOR; SECRETORY LEUKOCYTE PROTEINASE INHIBITOR;

EID: 0031560771     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.0983     Document Type: Article
Times cited : (42)

References (47)
  • 1
    • 0011219524 scopus 로고
    • Global and local secondary structures of globular proteins: Linking spectroscopies and predictions
    • Kluwer Academic Press
    • Alix A. J. P., Goulyaev D., Efremov R. Global and local secondary structures of globular proteins: linking spectroscopies and predictions. Spectroscopy of Biological Molecules. 1995;Kluwer Academic Press.
    • (1995) Spectroscopy of Biological Molecules
    • Alix, A.J.P.1    Goulyaev, D.2    Efremov, R.3
  • 2
    • 0026795399 scopus 로고
    • Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures
    • Berndt K. D., Güntert P., Orbons L. P. M., Wüthrich K. 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. 227:1992;757-775.
    • (1992) J. Mol. Biol. , vol.227 , pp. 757-775
    • Berndt, K.D.1    Güntert, P.2    Orbons, L.P.M.3    Wüthrich, K.4
  • 4
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W., Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204:1992;433-451.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 5
    • 0024571818 scopus 로고
    • Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors
    • Bode W., Meyer E., Jr, Powers J. C. Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors. Biochemistry. 28:1989;1951-1963.
    • (1989) Biochemistry , vol.28 , pp. 1951-1963
    • Bode, W.1    Meyer E., Jr.2    Powers, J.C.3
  • 7
    • 0024846405 scopus 로고
    • Use of restrained molecular dynamics in water to determine three-dimensional protein structure: Prediction of the three-dimensional structure ofEcballium elaterium
    • Chiche L., Gaboriaud C., Heitz A., Mornon J.-P., Castro B., Kollman P. A. Use of restrained molecular dynamics in water to determine three-dimensional protein structure: prediction of the three-dimensional structure ofEcballium elaterium. Proteins: Struct. Funct. Genet. 6:1989;405-417.
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 405-417
    • Chiche, L.1    Gaboriaud, C.2    Heitz, A.3    Mornon, J.-P.4    Castro, B.5    Kollman, P.A.6
  • 8
    • 0025871254 scopus 로고
    • Structures of larger proteins in solution: Three- and four-dimensional heteronuclear nmr spectroscopy
    • Clore G. M., Gronenborn A. M. Structures of larger proteins in solution: three- and four-dimensional heteronuclear nmr spectroscopy. Science. 252:1991;1390-1399.
    • (1991) Science , vol.252 , pp. 1390-1399
    • Clore, G.M.1    Gronenborn, A.M.2
  • 12
    • 0018900261 scopus 로고
    • The toxin-agglutinin fold. A new group of small protein structure organized around a four-disulfide core
    • Drenth J., Low B. W., Richardson J. S., Wright C. S. The toxin-agglutinin fold. A new group of small protein structure organized around a four-disulfide core. J. Biol. Chem. 255:1980;2652-2655.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2652-2655
    • Drenth, J.1    Low, B.W.2    Richardson, J.S.3    Wright, C.S.4
  • 14
    • 0023890859 scopus 로고
    • Human mucous proteinase inhibitor (human MPI). Human seminal inhibitor I (HUSI-I), antileukoprotease (ALP), secretory leukocyte protease inhibitor (SLPI)
    • Fritz H. Human mucous proteinase inhibitor (human MPI). Human seminal inhibitor I (HUSI-I), antileukoprotease (ALP), secretory leukocyte protease inhibitor (SLPI). Biol. Chem. Hoppe-Seyler. 369:1988;79-82.
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 79-82
    • Fritz, H.1
  • 15
    • 0024418787 scopus 로고
    • Slow isomerization of some proline-containing peptides inducing peak splitting during reversed-phase high-performance liquid chromatography
    • Gesquiere J.-C., Diesis E., Cung M. T., Tartar A. Slow isomerization of some proline-containing peptides inducing peak splitting during reversed-phase high-performance liquid chromatography. J. Chromatog. 478:1989;121-129.
    • (1989) J. Chromatog. , vol.478 , pp. 121-129
    • Gesquiere, J.-C.1    Diesis, E.2    Cung, M.T.3    Tartar, A.4
  • 16
    • 0040469390 scopus 로고
    • The 2.5 Å X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine α-chymotrypsin
    • Grütter M. G., Fendrich G., Huber R., Bode W. The 2.5 Å X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine α-chymotrypsin. EMBO J. 7:1988;345-351.
    • (1988) EMBO J. , vol.7 , pp. 345-351
    • Grütter, M.G.1    Fendrich, G.2    Huber, R.3    Bode, W.4
  • 17
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 18
    • 0027236599 scopus 로고
    • Determination of the disulphide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data. Application to flavoridin
    • Klaus W., Broger C., Gerber P., Senn H. Determination of the disulphide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data. Application to flavoridin. J. Mol. Biol. 232:1993;897-906.
    • (1993) J. Mol. Biol. , vol.232 , pp. 897-906
    • Klaus, W.1    Broger, C.2    Gerber, P.3    Senn, H.4
  • 19
    • 0029940321 scopus 로고    scopus 로고
    • Inhibition of human leukocyte and porcine pancreatic elastase by homologues of bovine pancreatic trypsin inhibitor
    • Kraunsoe J. A. E., Claridge T. D. W., Lowe G. Inhibition of human leukocyte and porcine pancreatic elastase by homologues of bovine pancreatic trypsin inhibitor. Biochemistry. 35:1996;9090-9096.
    • (1996) Biochemistry , vol.35 , pp. 9090-9096
    • Kraunsoe, J.A.E.1    Claridge, T.D.W.2    Lowe, G.3
  • 20
    • 0027980217 scopus 로고
    • Solution structure of turkey ovomucoid third domain as determined from nuclear magnetic resonance data
    • Krezel A. M., Darba P., Robertson A. D., Fejzo J., Macura S., Markley J. L. Solution structure of turkey ovomucoid third domain as determined from nuclear magnetic resonance data. J. Mol. Biol. 242:1994;203-214.
    • (1994) J. Mol. Biol. , vol.242 , pp. 203-214
    • Krezel, A.M.1    Darba, P.2    Robertson, A.D.3    Fejzo, J.4    Macura, S.5    Markley, J.L.6
  • 21
  • 22
    • 0000389264 scopus 로고
    • Use of a water flip-back pulse in the homonuclear NOESY experiment
    • Lippens G., Dhalluin C., Wieruszeski J. M. Use of a water flip-back pulse in the homonuclear NOESY experiment. J. Biomol. NMR. 5:1995;327-331.
    • (1995) J. Biomol. NMR , vol.5 , pp. 327-331
    • Lippens, G.1    Dhalluin, C.2    Wieruszeski, J.M.3
  • 23
    • 0029168711 scopus 로고
    • Structural, biochemical, and cell biological aspects of the serine proteinase inhibitor SKALP/elafin/ESI
    • Molhuizen H. O. F., Schalkwijk J. Structural, biochemical, and cell biological aspects of the serine proteinase inhibitor SKALP/elafin/ESI. Biol. Chem. Hoppe-Seyler. 376:1995;1-7.
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 1-7
    • Molhuizen, H.O.F.1    Schalkwijk, J.2
  • 24
    • 0027173236 scopus 로고
    • SKALP/elafin: An elastase inhibitor from cultured human keratinocytes. Purification, cDNA sequence, and evidence for transglutaminase cross-linking
    • Molhuizen H. O. F., Alkemade H. A. C., Zeeuwen P. L. J. M., de Jongh G. J., Wieringa B., Schalkwijk J. SKALP/elafin: an elastase inhibitor from cultured human keratinocytes. Purification, cDNA sequence, and evidence for transglutaminase cross-linking. J. Biol. Chem. 268:1993;12028-12032.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12028-12032
    • Molhuizen, H.O.F.1    Alkemade, H.A.C.2    Zeeuwen, P.L.J.M.3    De Jongh, G.J.4    Wieringa, B.5    Schalkwijk, J.6
  • 25
    • 0027155345 scopus 로고
    • Disulfide bond isomerization in BPTI and BPTI (G36S): An NMR study of correlated mobility in proteins
    • Otting G., Liepinsh E., Wüthrich K. Disulfide bond isomerization in BPTI and BPTI (G36S): an NMR study of correlated mobility in proteins. Biochemistry. 32:1993;3571-3582.
    • (1993) Biochemistry , vol.32 , pp. 3571-3582
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 27
    • 0029925433 scopus 로고    scopus 로고
    • Significance of secondary structure predictions on the reactive center loop region of serpins: A model for the folding of serpins into a metastable state
    • Patston P. A., Gettins P. G. W. Significance of secondary structure predictions on the reactive center loop region of serpins: a model for the folding of serpins into a metastable state. FEBS Letters. 383:1996;87-92.
    • (1996) FEBS Letters , vol.383 , pp. 87-92
    • Patston, P.A.1    Gettins, P.G.W.2
  • 28
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 29
    • 0019873820 scopus 로고
    • Estimation of globular secondary structure prediction from circular dichroism
    • Provencher S., Glöckner J. Estimation of globular secondary structure prediction from circular dichroism. Biochemistry. 20:1981;33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.1    Glöckner, J.2
  • 30
    • 0026631695 scopus 로고
    • Primary structure of the human elafin precursor preproelafin deduced from the nucleotide sequence of its gene and the presence of unique repetitive sequences in the prosegment
    • Saheki T., Ito F., Hagiwara H., Saito Y., Kuroki J., Tachibana S., Hirose S. Primary structure of the human elafin precursor preproelafin deduced from the nucleotide sequence of its gene and the presence of unique repetitive sequences in the prosegment. Biochem. Biophys. Res. Commun. 185:1992;240-245.
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 240-245
    • Saheki, T.1    Ito, F.2    Hagiwara, H.3    Saito, Y.4    Kuroki, J.5    Tachibana, S.6    Hirose, S.7
  • 31
    • 0025970641 scopus 로고
    • Purification and characterization of elastase-specific inhibitor. Sequence homology with mucous proteinase inhibitor
    • Sallenave J.-M., Ryle A. P. Purification and characterization of elastase-specific inhibitor. Sequence homology with mucous proteinase inhibitor. Biol. Chem. Hoppe-Seyler. 372:1991;13-21.
    • (1991) Biol. Chem. Hoppe-Seyler , vol.372 , pp. 13-21
    • Sallenave, J.-M.1    Ryle, A.P.2
  • 32
    • 0026493036 scopus 로고
    • Isolation of elafin and elastase-specific inhibitor (ESI) from bronchial secretions. Evidence of sequence homology and immunological cross-reactivity
    • Sallenave J.-M., Marsden M. D., Ryle A. P. Isolation of elafin and elastase-specific inhibitor (ESI) from bronchial secretions. Evidence of sequence homology and immunological cross-reactivity. Biol. Chem. Hoppe-Seyler. 373:1992;27-33.
    • (1992) Biol. Chem. Hoppe-Seyler , vol.373 , pp. 27-33
    • Sallenave, J.-M.1    Marsden, M.D.2    Ryle, A.P.3
  • 33
    • 0025347444 scopus 로고
    • Skin-derived antileukoproteinases (SKALPs): Characterization of two new elastase inhibitors from psoriatic epidermis
    • Schalkwijk J., Chang A., Janssen P., de Jongh G. J., Mier P. D. Skin-derived antileukoproteinases (SKALPs): characterization of two new elastase inhibitors from psoriatic epidermis. Br. J. Dermatol. 122:1990;631-641.
    • (1990) Br. J. Dermatol. , vol.122 , pp. 631-641
    • Schalkwijk, J.1    Chang, A.2    Janssen, P.3    De Jongh, G.J.4    Mier, P.D.5
  • 34
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:1967;157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 35
    • 0022479785 scopus 로고
    • The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease). Complete amino acid sequence as revealed by protein and cDNA sequencing and structural homology to whey proteins and Red Sea turtle proteinase inhibitor
    • Seemüller U., Arnhold M., Fritz H., Wiedenmann K., Machleidt W., Heinzel R., Appelhans H., Gassen H.-G., Lottspeich F. The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease). Complete amino acid sequence as revealed by protein and cDNA sequencing and structural homology to whey proteins and Red Sea turtle proteinase inhibitor. FEBS Letters. 199:1986;43-48.
    • (1986) FEBS Letters , vol.199 , pp. 43-48
    • Seemüller, U.1    Arnhold, M.2    Fritz, H.3    Wiedenmann, K.4    Machleidt, W.5    Heinzel, R.6    Appelhans, H.7    Gassen, H.-G.8    Lottspeich, F.9
  • 36
    • 0024391832 scopus 로고
    • Conformation of β-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering
    • Sibanda B. L., Blundell T. L., Thornton J. M. Conformation of β-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering. J. Mol. Biol. 206:1989;759-777.
    • (1989) J. Mol. Biol. , vol.206 , pp. 759-777
    • Sibanda, B.L.1    Blundell, T.L.2    Thornton, J.M.3
  • 38
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic Pancreatic Trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner G., Braun W., Havel T. F., Schaumann T., Go N., Wüthrich K. Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic Pancreatic Trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196:1987;611-639.
    • (1987) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Schaumann, T.4    Go, N.5    Wüthrich, K.6
  • 39
    • 43949164434 scopus 로고
    • A simple experimental scheme using pulsed field gradients for coherence-pathway rejection and solvent suppression in phase-sensitive heteronuclear correlation spectra
    • Wider G., Wüthrich K. A simple experimental scheme using pulsed field gradients for coherence-pathway rejection and solvent suppression in phase-sensitive heteronuclear correlation spectra. J. Magn. Reson. Ser. B. 102:1993;239-241.
    • (1993) J. Magn. Reson. Ser. B , vol.102 , pp. 239-241
    • Wider, G.1    Wüthrich, K.2
  • 40
    • 0025168332 scopus 로고
    • Elafin: An elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence
    • Wiedow O., Schröder J.-M., Gregory H., Young J. A., Christophers E. Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence. J. Biol. Chem. 265:1990;14791-14795.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14791-14795
    • Wiedow, O.1    Schröder, J.-M.2    Gregory, H.3    Young, J.A.4    Christophers, E.5
  • 42
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of β-turn in proteins
    • Wilmot C. M., Thornton J. M. Analysis and prediction of the different types of β-turn in proteins. J. Mol. Biol. 203:1988;221-232.
    • (1988) J. Mol. Biol. , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 44
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart D. S., Sykes B. D., Richards F. M. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 31:1992;1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 46
    • 0027406841 scopus 로고
    • Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin
    • Ying Q.-L., Simon S. R. Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin. Biochemistry. 32:1993;1866-1874.
    • (1993) Biochemistry , vol.32 , pp. 1866-1874
    • Ying, Q.-L.1    Simon, S.R.2
  • 47
    • 0028199929 scopus 로고
    • Functions of the N-terminal domain of secretory leukoprotease inhibitor
    • Ying Q.-L., Kemme M., Simon S. R. Functions of the N-terminal domain of secretory leukoprotease inhibitor. Biochemistry. 33:1994;5445-5450.
    • (1994) Biochemistry , vol.33 , pp. 5445-5450
    • Ying, Q.-L.1    Kemme, M.2    Simon, S.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.