메뉴 건너뛰기




Volumn 132, Issue 2-3, 2008, Pages 159-164

Structural characterization and low-resolution model of BJ-48, a thrombin-like enzyme from Bothrops jararacussu venom

Author keywords

pH induced conformational changes; Protein shape; Serine protease; Snake venom; Solution structure; SVTLE

Indexed keywords

BATROXOBIN; BOTHROPS JARARACUSSU VENOM; PROTEIN BJ 48; SERINE PROTEINASE; SNAKE VENOM; THROMBIN; UNCLASSIFIED DRUG;

EID: 37049002682     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2007.11.002     Document Type: Article
Times cited : (4)

References (20)
  • 2
    • 19544394247 scopus 로고    scopus 로고
    • Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved
    • Serrano S.M., and Maroun R.C. Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved. Toxicon 45 (2005) 1115-1132
    • (2005) Toxicon , vol.45 , pp. 1115-1132
    • Serrano, S.M.1    Maroun, R.C.2
  • 3
    • 2142750129 scopus 로고    scopus 로고
    • S1 subsite in snake venom thrombin-like enzymes: can S1 subsite lipophilicity be used to sort binding affinities of trypsin-like enzymes to small-molecule inhibitors?
    • (Erratum in: Bioorg. Med. Chem. 12 (2004) 3755)
    • Silva Jr. F.P., and De-Simone S.G. S1 subsite in snake venom thrombin-like enzymes: can S1 subsite lipophilicity be used to sort binding affinities of trypsin-like enzymes to small-molecule inhibitors?. Bioorg. Med. Chem. 12 (2004) 2571-2587 (Erratum in: Bioorg. Med. Chem. 12 (2004) 3755)
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 2571-2587
    • Silva Jr., F.P.1    De-Simone, S.G.2
  • 4
    • 0029962944 scopus 로고    scopus 로고
    • Conservation and variability in the structures of serine proteinases of the chymotrypsin family
    • Lesk A.M., and Fordham W.D. Conservation and variability in the structures of serine proteinases of the chymotrypsin family. J. Mol. Biol. 258 (1996) 501-537
    • (1996) J. Mol. Biol. , vol.258 , pp. 501-537
    • Lesk, A.M.1    Fordham, W.D.2
  • 5
    • 0035844698 scopus 로고    scopus 로고
    • Structural features of a snake venom thrombin-like enzyme: thrombin and trypsin on a single catalytic platform?
    • Castro H.C., Silva D.M., Craik C., and Zingali R.B. Structural features of a snake venom thrombin-like enzyme: thrombin and trypsin on a single catalytic platform?. Biochim. Biophys. Acta 1547 (2001) 183-195
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 183-195
    • Castro, H.C.1    Silva, D.M.2    Craik, C.3    Zingali, R.B.4
  • 6
    • 34249744642 scopus 로고    scopus 로고
    • BJ-48, a novel thrombin-like enzyme from the Bothrops jararacussu venom with high selectivity for Arg over Lys in P1: role of N-glycosylation
    • Silva Jr. F.P., Guedes H.L.M., Garvey L.C., Aguiard A.S., Bourguignon S.C., Di Cera E., and Giovanni-De-Simone S. BJ-48, a novel thrombin-like enzyme from the Bothrops jararacussu venom with high selectivity for Arg over Lys in P1: role of N-glycosylation. Toxicon 50 (2007) 18-31
    • (2007) Toxicon , vol.50 , pp. 18-31
    • Silva Jr., F.P.1    Guedes, H.L.M.2    Garvey, L.C.3    Aguiard, A.S.4    Bourguignon, S.C.5    Di Cera, E.6    Giovanni-De-Simone, S.7
  • 7
    • 0029851195 scopus 로고    scopus 로고
    • Temperature and pH sensitivity of trypsins from atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin
    • Outzen H., Berglund I.G., Smalas A.O., and Willassen N.P. Temperature and pH sensitivity of trypsins from atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin. Comp. Biochem. Physiol. 115 (1996) 33-45
    • (1996) Comp. Biochem. Physiol. , vol.115 , pp. 33-45
    • Outzen, H.1    Berglund, I.G.2    Smalas, A.O.3    Willassen, N.P.4
  • 8
    • 0043135137 scopus 로고    scopus 로고
    • Characterization of p-aminobenzamidine-based sorbent and its use for high-performance affinity chromatography of trypsin-like proteases
    • Nakamura K., Suzuki T., Hasegawa M., Kato Y., Sasaki H., and Inouye K. Characterization of p-aminobenzamidine-based sorbent and its use for high-performance affinity chromatography of trypsin-like proteases. J. Chromatogr. A 1009 (2003) 133-139
    • (2003) J. Chromatogr. A , vol.1009 , pp. 133-139
    • Nakamura, K.1    Suzuki, T.2    Hasegawa, M.3    Kato, Y.4    Sasaki, H.5    Inouye, K.6
  • 9
    • 22244493880 scopus 로고    scopus 로고
    • Biochemical and molecular modeling analysis of the ability of two p-aminobenzamidine-based sorbents to selectively purify serine proteases (fibrinogenases) from snake venoms
    • De-Simone S.G., Correa-Netto C., Antunes O.A.C., De-Alencastro R.B., and Silva Jr. F.P. Biochemical and molecular modeling analysis of the ability of two p-aminobenzamidine-based sorbents to selectively purify serine proteases (fibrinogenases) from snake venoms. J. Chromatogr. B 822 (2005) 1-9
    • (2005) J. Chromatogr. B , vol.822 , pp. 1-9
    • De-Simone, S.G.1    Correa-Netto, C.2    Antunes, O.A.C.3    De-Alencastro, R.B.4    Silva Jr., F.P.5
  • 12
    • 0026244044 scopus 로고
    • GNOM-a program package for small-angle scattering data processing
    • Semenyuk V., and Svergun D.I. GNOM-a program package for small-angle scattering data processing. J. Appl. Crystallogr. 24 (1991) 537-540
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 537-540
    • Semenyuk, V.1    Svergun, D.I.2
  • 13
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun D.I., Petoukhov M.V., and Koch M.H. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80 (2001) 2946-2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 14
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia De La Torre J., Huertas M.L., and Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78 (2000) 719-730
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 15
    • 4544240366 scopus 로고    scopus 로고
    • New insights into conformational and functional stability of human alpha-thrombin probed by high hydrostatic pressure
    • Lima L.M., Zingali R.B., Foguel D., and Monteiro R.Q. New insights into conformational and functional stability of human alpha-thrombin probed by high hydrostatic pressure. Eur. J. Biochem. 271 (2004) 3580-3587
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3580-3587
    • Lima, L.M.1    Zingali, R.B.2    Foguel, D.3    Monteiro, R.Q.4
  • 16
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov V.V., and Svergun D.I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36 (2003) 860-864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 17
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: a point where biology waits for physics
    • Uversky V.N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 11 (2002) 739-756
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 18
    • 0024431034 scopus 로고
    • The refined 1.9 Å crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode V., Mayr V., Baumann U., Huber R., Stone S.R., and Hofsteenge J. The refined 1.9 Å crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J. 8 (1989) 3467-3475
    • (1989) EMBO J. , vol.8 , pp. 3467-3475
    • Bode, V.1    Mayr, V.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 19
    • 0016796849 scopus 로고
    • The refined crystal structure of bovine beta-trypsin at 1.8 Å resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0
    • Bode W., and Schwager P. The refined crystal structure of bovine beta-trypsin at 1.8 Å resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0. J. Mol. Biol. 98 (1975) 693-717
    • (1975) J. Mol. Biol. , vol.98 , pp. 693-717
    • Bode, W.1    Schwager, P.2
  • 20
    • 3042743892 scopus 로고    scopus 로고
    • Metal-ion-and pH-induced conformational changes of acutolysin D from Agkistrodon acutus venom probed by fluorescent spectroscopy
    • Xu X.L., Liu X.H., Wu B., Liu Y., Liu W.Q., Xie Y.S., and Liu Q.L. Metal-ion-and pH-induced conformational changes of acutolysin D from Agkistrodon acutus venom probed by fluorescent spectroscopy. Biopolymers 74 (2004) 336-344
    • (2004) Biopolymers , vol.74 , pp. 336-344
    • Xu, X.L.1    Liu, X.H.2    Wu, B.3    Liu, Y.4    Liu, W.Q.5    Xie, Y.S.6    Liu, Q.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.