메뉴 건너뛰기




Volumn 45, Issue 8, 2005, Pages 1063-1074

Snake venom disintegrins: Evolution of structure and function

Author keywords

Disintegrins; Disulfide bond engineering; Evolution of protein structure; Integrin antagonists; Snake venom proteins; Structure function correlations

Indexed keywords

DISINTEGRIN; INTEGRIN RECEPTOR; PROTEIN SUBUNIT; SNAKE VENOM; VERY LATE ACTIVATION ANTIGEN 1; VIPER VENOM;

EID: 19544381539     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2005.02.024     Document Type: Article
Times cited : (237)

References (69)
  • 2
    • 4344607978 scopus 로고    scopus 로고
    • Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 Å resolution
    • S. Bilgrami, S. Tomar, S. Yadav, P. Kaur, J. Kumar, T. Jabeen, S. Sharma, and T.P. Sinhg Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 Å resolution J. Mol. Biol. 341 2004 829 837
    • (2004) J. Mol. Biol. , vol.341 , pp. 829-837
    • Bilgrami, S.1    Tomar, S.2    Yadav, S.3    Kaur, P.4    Kumar, J.5    Jabeen, T.6    Sharma, S.7    Sinhg, T.P.8
  • 3
    • 0028146808 scopus 로고
    • Hemorrhagic metalloproteinases from snake venoms
    • J.B. Bjarnason, and J.W. Fox Hemorrhagic metalloproteinases from snake venoms Pharmac. Ther. 62 1994 325 372
    • (1994) Pharmac. Ther. , vol.62 , pp. 325-372
    • Bjarnason, J.B.1    Fox, J.W.2
  • 4
    • 0016631388 scopus 로고
    • Binding of flexible ligands to macromolecules
    • A.S.V. Burgen, G.C.K. Roberts, and J. Freeney Binding of flexible ligands to macromolecules Nature 253 1975 753 755
    • (1975) Nature , vol.253 , pp. 753-755
    • Burgen, A.S.V.1    Roberts, G.C.K.2    Freeney, J.3
  • 5
    • 0025914382 scopus 로고
    • Identification of the disulfide bond pattern in albolabrin, an RGD-containing peptide from the venom of Trimeresurus albolabris: Significance for the expression of platelet aggregation inhibitory activity
    • J.J. Calvete, W. Schäfer, T. Soszka, W. Lu, J.J. Cook, B.A. Jameson, and S. Niewiarowski Identification of the disulfide bond pattern in albolabrin, an RGD-containing peptide from the venom of Trimeresurus albolabris: significance for the expression of platelet aggregation inhibitory activity Biochemistry 30 1991 5225 5229
    • (1991) Biochemistry , vol.30 , pp. 5225-5229
    • Calvete, J.J.1    Schäfer, W.2    Soszka, T.3    Lu, W.4    Cook, J.J.5    Jameson, B.A.6    Niewiarowski, S.7
  • 9
    • 0037591683 scopus 로고    scopus 로고
    • Snake venom disintegrins: Novel dimeric disintegrins and structural diversification by disulfide bond engineering
    • J.J. Calvete, M.P. Moreno-Murciano, R.D.G. Theakston, D.G. Kisiel, and C. Marcinkiewicz Snake venom disintegrins: novel dimeric disintegrins and structural diversification by disulfide bond engineering Biochem. J. 372 2003 725 734
    • (2003) Biochem. J. , vol.372 , pp. 725-734
    • Calvete, J.J.1    Moreno-Murciano, M.P.2    Theakston, R.D.G.3    Kisiel, D.G.4    Marcinkiewicz, C.5
  • 11
    • 13044283060 scopus 로고    scopus 로고
    • Developmental shifts and species selection in gastropods
    • T.F. Duda jr, and S.R. Palumbi Developmental shifts and species selection in gastropods Proc. Natl Acad. Sci. USA 96 1999 6820 6823
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6820-6823
    • Duda Jr., T.F.1    Palumbi, S.R.2
  • 13
    • 0002655721 scopus 로고    scopus 로고
    • The ADAMs/MDC family of proteins and their relationships to the snake venom metalloproteinases
    • G.S. Bailey Alaken Press Ft. Collins, Co, USA
    • J.W. Fox, and C. Long The ADAMs/MDC family of proteins and their relationships to the snake venom metalloproteinases G.S. Bailey Snake Venom Enzymes 1998 Alaken Press Ft. Collins, Co, USA 151 178
    • (1998) Snake Venom Enzymes , pp. 151-178
    • Fox, J.W.1    Long, C.2
  • 14
    • 0032889728 scopus 로고    scopus 로고
    • Structure-function properties of venom components from Australian elapids
    • B.G. Fry Structure-function properties of venom components from Australian elapids Toxicon 37 1999 11 32
    • (1999) Toxicon , vol.37 , pp. 11-32
    • Fry, B.G.1
  • 15
    • 0042887427 scopus 로고    scopus 로고
    • Crystal structure of trimestatin, a disintegrin containing a cell adhesion recognition motif RGD
    • Y. Fujii, D. Okuda, Z. Fujimoto, K. Horii, T. Morita, and H. Mizuno Crystal structure of trimestatin, a disintegrin containing a cell adhesion recognition motif RGD J. Mol. Biol. 332 2003 1115 1122
    • (2003) J. Mol. Biol. , vol.332 , pp. 1115-1122
    • Fujii, Y.1    Okuda, D.2    Fujimoto, Z.3    Horii, K.4    Morita, T.5    Mizuno, H.6
  • 17
    • 0026748687 scopus 로고
    • Sequence of a cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: Evidence for signal, zymogen, and disintegrin-like structures
    • L.A. Hite, J.D. Shannon, J.B. Bjarnason, and J.W. Fox Sequence of a cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: evidence for signal, zymogen, and disintegrin-like structures Biochemistry 31 1992 6203 6211
    • (1992) Biochemistry , vol.31 , pp. 6203-6211
    • Hite, L.A.1    Shannon, J.D.2    Bjarnason, J.B.3    Fox, J.W.4
  • 18
    • 0028337108 scopus 로고
    • cDNA sequences of four snake venom metalloproteinases: Structure, classification, and their relationship to mammalian reproductive proteins
    • L.A. Hite, L-G. Jia, J.B. Bjarnason, and J.W. Fox cDNA sequences of four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins Arch. Biochem. Biophys. 308 1994 182 191
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 182-191
    • Hite, L.A.1    Jia, L-G.2    Bjarnason, J.B.3    Fox, J.W.4
  • 19
    • 0036290784 scopus 로고    scopus 로고
    • Structural and functional significance of disulfide bonds in saxatilin, a 7.7 kDa disintegrin
    • S.-Y. Hong, Y.-D. Sohn, K.-H. Chung, and D.-S. Kim Structural and functional significance of disulfide bonds in saxatilin, a 7.7 kDa disintegrin Biochem. Biophys. Res. Commun. 293 2002 530 536
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 530-536
    • Hong, S.-Y.1    Sohn, Y.-D.2    Chung, K.-H.3    Kim, D.-S.4
  • 20
    • 0023639428 scopus 로고
    • Trigramin. A low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex
    • T.-F. Huang, J.C. Holt, H. Lukasiewicz, and S. Niewiarowski Trigramin. A low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex J. Biol. Chem. 262 1987 16157 16163
    • (1987) J. Biol. Chem. , vol.262 , pp. 16157-16163
    • Huang, T.-F.1    Holt, J.C.2    Lukasiewicz, H.3    Niewiarowski, S.4
  • 21
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • R.O. Hynes Integrins: bidirectional, allosteric signaling machines Cell 110 2002 673 687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 23
    • 0030273873 scopus 로고    scopus 로고
    • Snake venom metalloproteinases: Structure, function and relationship to the ADAMs family of proteins
    • L-G. Jia, K-i Shimokawa, J.B. Bjarnason, and J.W. Fox Snake venom metalloproteinases: structure, function and relationship to the ADAMs family of proteins Toxicon 34 1996 1269 1276
    • (1996) Toxicon , vol.34 , pp. 1269-1276
    • Jia, L-G.1    Shimokawa K-i2    Bjarnason, J.B.3    Fox, J.W.4
  • 24
    • 0030976889 scopus 로고    scopus 로고
    • Function of disintegrin-like/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists
    • L.-G. Jia, X.-M. Wang, J.D. Shannon, J.B. Bjarnason, and J.W. Fox Function of disintegrin-like/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists J. Biol. Chem. 272 1997 13094 13102
    • (1997) J. Biol. Chem. , vol.272 , pp. 13094-13102
    • Jia, L.-G.1    Wang, X.-M.2    Shannon, J.D.3    Bjarnason, J.B.4    Fox, J.W.5
  • 25
    • 0033958729 scopus 로고    scopus 로고
    • Inhibition of platelet aggregation by the recombinant cysteine-rich domain of the hemorrhagic snake venom metalloproteinase, atrolysin A
    • L.-G. Jia, X.-M. Wang, J.D. Shannon, J.B. Bjarnason, and J.W. Fox Inhibition of platelet aggregation by the recombinant cysteine-rich domain of the hemorrhagic snake venom metalloproteinase, atrolysin A Arch. Biochem. Biophys. 373 2000 281 286
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 281-286
    • Jia, L.-G.1    Wang, X.-M.2    Shannon, J.D.3    Bjarnason, J.B.4    Fox, J.W.5
  • 26
    • 1242316947 scopus 로고    scopus 로고
    • Snake venomics: Characterization of protein families in Sistrurus barbouri venom by cysteine mapping, N-terminal sequencing, and MS/MS analysis
    • P. Juárez, L. Sanz, and J.J. Calvete Snake venomics: characterization of protein families in Sistrurus barbouri venom by cysteine mapping, N-terminal sequencing, and MS/MS analysis Proteomics 4 2004 327 338
    • (2004) Proteomics , vol.4 , pp. 327-338
    • Juárez, P.1    Sanz, L.2    Calvete, J.J.3
  • 27
    • 0029949611 scopus 로고
    • 1 integrin by the snake venom metalloprotease jararhagin
    • 1 integrin by the snake venom metalloprotease jararhagin Biochem. J. 320 1995 635 641
    • (1995) Biochem. J. , vol.320 , pp. 635-641
    • Kamiguti, A.S.1    Hay, C.R.M.2    Zuzel, M.3
  • 28
    • 0042564783 scopus 로고    scopus 로고
    • Identification of sites in the cysteine-rich domain of the class P-III snake venom metalloproteinases responsible for inhibition of platelet function
    • A.S. Kamiguti, P. Gallagher, C. Marcinkiewicz, R.D.G. Theakston, M. Zuzel, and J.W. Fox Identification of sites in the cysteine-rich domain of the class P-III snake venom metalloproteinases responsible for inhibition of platelet function FEBS Lett. 549 2003 129 134
    • (2003) FEBS Lett. , vol.549 , pp. 129-134
    • Kamiguti, A.S.1    Gallagher, P.2    Marcinkiewicz, C.3    Theakston, R.D.G.4    Zuzel, M.5    Fox, J.W.6
  • 29
    • 0026506731 scopus 로고
    • Structural domains in venom proteins: Evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor
    • R.M. Kini, and H.J. Evans Structural domains in venom proteins: evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor Toxicon 30 1992 265 293
    • (1992) Toxicon , vol.30 , pp. 265-293
    • Kini, R.M.1    Evans, H.J.2
  • 30
    • 0038770146 scopus 로고    scopus 로고
    • Functional diversification of animal toxins by adaptative evolution
    • A. Ménez Wiley New York
    • D. Kordis, I. Krizaj, and F. Gubensek Functional diversification of animal toxins by adaptative evolution A. Ménez Perspectives in Molecular Toxinology 2002 Wiley New York 401 419
    • (2002) Perspectives in Molecular Toxinology , pp. 401-419
    • Kordis, D.1    Krizaj, I.2    Gubensek, F.3
  • 31
    • 0030042941 scopus 로고    scopus 로고
    • Substitutions of proline 42 to alanine and methionine 46 to asparagine around the RGD domain of the neurotoxin dendroaspin alter its preferential antagonism to that resembling the disintegrin elegantin
    • X. Lu, S. Rahman, V.V. Kakkar, and K.S. Authi Substitutions of proline 42 to alanine and methionine 46 to asparagine around the RGD domain of the neurotoxin dendroaspin alter its preferential antagonism to that resembling the disintegrin elegantin J. Biol. Chem. 271 1996 289 294
    • (1996) J. Biol. Chem. , vol.271 , pp. 289-294
    • Lu, X.1    Rahman, S.2    Kakkar, V.V.3    Authi, K.S.4
  • 37
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • F.S. Markland Snake venoms and the hemostatic system Toxicon 36 1998 1749 1800
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland, F.S.1
  • 41
    • 0242664789 scopus 로고    scopus 로고
    • Concerted motions of the integrin-binding loop and the c-terminal tail of the non-RGD disintegrin obtustatin
    • D. Monleón, M.P. Moreno-Murciano, H. Kovacs, C. Marcinkiewicz, J.J. Calvete, and B. Celda Concerted motions of the integrin-binding loop and the c-terminal tail of the non-RGD disintegrin obtustatin J. Biol. Chem. 278 2003 45570 45576
    • (2003) J. Biol. Chem. , vol.278 , pp. 45570-45576
    • Monleón, D.1    Moreno-Murciano, M.P.2    Kovacs, H.3    Marcinkiewicz, C.4    Calvete, J.J.5    Celda, B.6
  • 42
    • 0037301510 scopus 로고    scopus 로고
    • Amino acid sequence and homology modeling of obtustatin, a novel non-RGD-containing short disintegrin isolated from the venom of Vipera lebetina obtusa
    • M.P. Moreno-Murciano, D. Monleón, J.J. Calvete, B. Celda, and C. Marcinkiewicz Amino acid sequence and homology modeling of obtustatin, a novel non-RGD-containing short disintegrin isolated from the venom of Vipera lebetina obtusa Protein Sci. 12 2003 366 371
    • (2003) Protein Sci. , vol.12 , pp. 366-371
    • Moreno-Murciano, M.P.1    Monleón, D.2    Calvete, J.J.3    Celda, B.4    Marcinkiewicz, C.5
  • 44
    • 0029814973 scopus 로고    scopus 로고
    • Evolution of disintegrin cysteine-rich and mammalian matrix-degrading metalloproteinases: Gene duplication and divergence of a common ancestor rather than convergent evolution
    • A.M. Moura da Silva, R.D.G. Theakston, and J.M. Crampton Evolution of disintegrin cysteine-rich and mammalian matrix-degrading metalloproteinases: gene duplication and divergence of a common ancestor rather than convergent evolution J. Mol. Evol. 43 1996 263 269
    • (1996) J. Mol. Evol. , vol.43 , pp. 263-269
    • Moura Da Silva, A.M.1    Theakston, R.D.G.2    Crampton, J.M.3
  • 47
    • 0034213348 scopus 로고    scopus 로고
    • Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom
    • T. Nikai, K. Taniguchi, Y. Komori, K. Masuda, J.W. Fox, and H. Sugihara Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom Arch. Biochem. Biophys. 378 2000 6 15
    • (2000) Arch. Biochem. Biophys. , vol.378 , pp. 6-15
    • Nikai, T.1    Taniguchi, K.2    Komori, Y.3    Masuda, K.4    Fox, J.W.5    Sugihara, H.6
  • 50
    • 0035049724 scopus 로고    scopus 로고
    • Comparative biochemistry of disintegrins isolated from snake venoms: Consideration of the taxonomy and geographical distribution of snakes in the genus Echis
    • D. Okuda, C. Nozaki, F. Sekiya, and T. Morita Comparative biochemistry of disintegrins isolated from snake venoms: consideration of the taxonomy and geographical distribution of snakes in the genus Echis J. Biochem. 129 2001 615 620
    • (2001) J. Biochem. , vol.129 , pp. 615-620
    • Okuda, D.1    Nozaki, C.2    Sekiya, F.3    Morita, T.4
  • 51
    • 0037016015 scopus 로고    scopus 로고
    • A new gene structure of the disintegrin family: A subunit of dimeric disintegrin has a short coding region
    • D. Okuda, H. Koike, and T. Morita A new gene structure of the disintegrin family: a subunit of dimeric disintegrin has a short coding region Biochemistry 41 2002 14248 14254
    • (2002) Biochemistry , vol.41 , pp. 14248-14254
    • Okuda, D.1    Koike, H.2    Morita, T.3
  • 52
    • 0033049456 scopus 로고    scopus 로고
    • Ussuristatin 2, a novel KGD-bearing disintegrin from Agkistrodon ussuriensis venom
    • K. Oshikawa, and S. Terada Ussuristatin 2, a novel KGD-bearing disintegrin from Agkistrodon ussuriensis venom J. Biochem. 125 1999 31 35
    • (1999) J. Biochem. , vol.125 , pp. 31-35
    • Oshikawa, K.1    Terada, S.2
  • 56
    • 0027165368 scopus 로고
    • The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GPIIb-IIIa receptor
    • H. Senn, and W. Klaus The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GPIIb-IIIa receptor J. Mol. Biol. 232 1993 907 925
    • (1993) J. Mol. Biol. , vol.232 , pp. 907-925
    • Senn, H.1    Klaus, W.2
  • 57
    • 0031195282 scopus 로고    scopus 로고
    • Sequence and biological activity of catrocollastatin-C: A disintegrin-like/cysteine-rich two domain protein from Crotalus atrox venom
    • K-I. Shimokawa, J.D. Shannon, L-G. Jia, and J.W. Fox Sequence and biological activity of catrocollastatin-C: a disintegrin-like/cysteine-rich two domain protein from Crotalus atrox venom Arch. Biochem. Biophys. 343 1997 35 43
    • (1997) Arch. Biochem. Biophys. , vol.343 , pp. 35-43
    • Shimokawa, K-I.1    Shannon, J.D.2    Jia, L-G.3    Fox, J.W.4
  • 58
    • 0032527059 scopus 로고    scopus 로고
    • Isolation, sequence analysis, and biological activity of atrolysin E/D, the non-RGD disintegrin domain from Crotalus atrox venom
    • K-i. Shimokawa, L-G. Jia, J.D. Shannon, and J.W. Fox Isolation, sequence analysis, and biological activity of atrolysin E/D, the non-RGD disintegrin domain from Crotalus atrox venom Arch. Biochem. Biophys. 354 1998 239 246
    • (1998) Arch. Biochem. Biophys. , vol.354 , pp. 239-246
    • Shimokawa, K-i.1    Jia, L-G.2    Shannon, J.D.3    Fox, J.W.4
  • 59
    • 0348111219 scopus 로고    scopus 로고
    • Solution structure of a novel disintegrin, salmosin, from Agkistrodon halys venom
    • J. Shin, S-Y. Hong, K. Chung, I. Kang, Y. Jang, D.-S. Kim, and W. Lee Solution structure of a novel disintegrin, salmosin, from Agkistrodon halys venom Biochemistry 42 2003 14408 14415
    • (2003) Biochemistry , vol.42 , pp. 14408-14415
    • Shin, J.1    Hong, S-Y.2    Chung, K.3    Kang, I.4    Jang, Y.5    Kim, D.-S.6    Lee, W.7
  • 63
    • 0024429207 scopus 로고
    • NMR studies of mobility within protein structure
    • R.J.P. Williams NMR studies of mobility within protein structure Eur. J. Biochem. 183 1989 479 497
    • (1989) Eur. J. Biochem. , vol.183 , pp. 479-497
    • Williams, R.J.P.1
  • 64
    • 0027308240 scopus 로고
    • An echistatin C-terminal peptide activates GPIIbIIIa binding to fibrinogen, fibronectin, vitronectin and collagen type I and type IV
    • P.S. Wright, V. Saudek, T.J. Owen, S.L. Harbeson, and A.J. Bitonti An echistatin C-terminal peptide activates GPIIbIIIa binding to fibrinogen, fibronectin, vitronectin and collagen type I and type IV Biochem. J. 293 1993 263 267
    • (1993) Biochem. J. , vol.293 , pp. 263-267
    • Wright, P.S.1    Saudek, V.2    Owen, T.J.3    Harbeson, S.L.4    Bitonti, A.J.5
  • 65
    • 0035423930 scopus 로고    scopus 로고
    • Purification, molecular cloning and mechanism of action of graminelysin I, a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells
    • W.B. Wu, S.C. Chang, M.Y. Liau, and T.F. Huang Purification, molecular cloning and mechanism of action of graminelysin I, a snake-venom-derived metalloproteinase that induces apoptosis of human endothelial cells Biochem. J. 357 2001 719 728
    • (2001) Biochem. J. , vol.357 , pp. 719-728
    • Wu, W.B.1    Chang, S.C.2    Liau, M.Y.3    Huang, T.F.4
  • 68
    • 0029105096 scopus 로고
    • Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen
    • Q. Zhou, J.B. Smith, and M.H. Grossman Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen Biochem. J. 307 1995 411 417
    • (1995) Biochem. J. , vol.307 , pp. 411-417
    • Zhou, Q.1    Smith, J.B.2    Grossman, M.H.3
  • 69
    • 0037174925 scopus 로고    scopus 로고
    • The reprolysin jararhagin, a snake venom metalloproteinase, functions as a fibrillar collagen agonist involved in fibroblast cell adhesion and signaling
    • P. Zigrino, A.S. Kamiguti, J. Eble, C. Drescher, R. Nischt, J.W. Fox, and C. Mauch The reprolysin jararhagin, a snake venom metalloproteinase, functions as a fibrillar collagen agonist involved in fibroblast cell adhesion and signaling J. Biol. Chem. 277 2002 40528 40535
    • (2002) J. Biol. Chem. , vol.277 , pp. 40528-40535
    • Zigrino, P.1    Kamiguti, A.S.2    Eble, J.3    Drescher, C.4    Nischt, R.5    Fox, J.W.6    Mauch, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.