Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities

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dc.contributor.authorWatanabe, L.
dc.contributor.authorShannon, J. D.
dc.contributor.authorValente, R. H.
dc.contributor.authorRucavado, A.
dc.contributor.authorAlape-Giron, A.
dc.contributor.authorKamiguti, A. S.
dc.contributor.authorTheakston, RDG
dc.contributor.authorFox, J. W.
dc.contributor.authorGutierrez, J. M.
dc.contributor.authorArni, R. K.
dc.contributor.institutionUniv Costa Rica
dc.contributor.institutionUniv Liverpool
dc.contributor.institutionFiocruz MS
dc.contributor.institutionUniversity of Virginia (UVA)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T14:02:24Z
dc.date.available2014-05-20T14:02:24Z
dc.date.issued2003-10-01
dc.description.abstractBaP1 is a 22.7-kD P-I-type zinc-dependent metalloproteinase isolated from the venom of the snake Bothrops asper, a medically relevant species in Central America. This enzyme exerts multiple tissue-damaging activities, including hemorrhage, myonecrosis, dermonecrosis, blistering, and edema. BaP1 is a single chain of 202 amino acids that shows highest sequence identity with metalloproteinases isolated front the venoms of snakes of the subfamily Crotalinae. It has six Cys residues involved in three disulfide bridges (Cys 117-Cys 197, Cys 159-Cys 181, Cys 157-Cys 164). It has the consensus sequence H(142)E(143)XXH(146)XXGXXH(152), as well as the sequence C164I165M166, which characterize the metzincin superfamily of metalloproteinases. The active-site cleft separates a major subdomain (residues 1-152), comprising four a-helices and a five-stranded beta-sheet, from the minor subdomain, which is formed by a single a-helix and several loops. The catalytic zinc ion is coordinated by the N-epsilon2 nitrogen atoms of His 142, His 146, and His 152, in addition to a solvent water molecule, which in turn is bound to Glu 143. Several conserved residues contribute to the formation of the hydrophobic pocket, and Met 166 serves as a hydrophobic base for the active-site groups. Sequence and structural comparisons of hemorrhagic and nonhemorrhagic P-I metalloproteinases from snake venoms revealed differences in several regions. In particular, the loop comprising residues 153 to 176 has marked structural differences between metalloproteinases with very different hemorrhagic activities. Because this region lies in close proximity to the active-site microenvironment, it may influence the interaction of these enzymes with physiologically relevant substrates in the extracellular matrix.en
dc.description.affiliationUniv Costa Rica, Fac Microbiol, Inst Clodomiro Picado, San Jose, Costa Rica
dc.description.affiliationUniv Costa Rica, Escuela Med, Dept Bioquim, San Jose, Costa Rica
dc.description.affiliationUniv Liverpool, Royal Liverpool Univ Hosp, Dept Haematol, Liverpool, Merseyside, England
dc.description.affiliationUniv Liverpool, Liverpool Sch Trop Med, Venom Res Unit, Liverpool L3 5QA, Merseyside, England
dc.description.affiliationFiocruz MS, Dept Fisiol & Farmacodinam, BR-21045900 Rio de Janeiro, Brazil
dc.description.affiliationUniv Virginia, Hlth Sci Ctr, Dept Microbiol, Charlottesville, VA 22908 USA
dc.description.affiliationUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, Brazil
dc.description.affiliationUnespUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, Brazil
dc.format.extent2273-2281
dc.identifierhttp://dx.doi.org/10.1110/ps.03102403
dc.identifier.citationProtein Science. Woodbury: Cold Spring Harbor Lab Press, Publications Dept, v. 12, n. 10, p. 2273-2281, 2003.
dc.identifier.doi10.1110/ps.03102403
dc.identifier.fileWOS000185425500016.pdf
dc.identifier.issn0961-8368
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/21996
dc.identifier.wosWOS:000185425500016
dc.language.isoeng
dc.publisherCold Spring Harbor Lab Press, Publications Dept
dc.relation.ispartofProtein Science
dc.relation.ispartofjcr2.410
dc.relation.ispartofsjr1,652
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectsnake venompt
dc.subjectzinc-dependent metalloproteinasespt
dc.subjectmetzincinspt
dc.subjecthemorrhagic toxinspt
dc.subjectamino acid sequencept
dc.subjectCrystal structurept
dc.titleAmino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activitiesen
dc.typeArtigo
dcterms.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dcterms.rightsHolderCold Spring Harbor Lab Press, Publications Dept
unesp.author.lattes9162508978945887[10]
unesp.author.orcid0000-0001-8385-3081[9]
unesp.author.orcid0000-0002-6562-7571[3]
unesp.author.orcid0000-0003-2460-1145[10]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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