Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom

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dc.contributor.authorMurakami, Mário T. [UNESP]
dc.contributor.authorMelo, Cristiane C. [UNESP]
dc.contributor.authorAngulo, Yamileth
dc.contributor.authorLomonte, Bruno
dc.contributor.authorArni, Raghuvir K. [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionFacultad de Microbiologia
dc.contributor.institutionUniversidad de Costa Rica
dc.contributor.institutionInstituto Butantan
dc.date.accessioned2014-05-27T11:21:51Z
dc.date.available2014-05-27T11:21:51Z
dc.date.issued2006-05-01
dc.description.abstractLys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic proteins which, although lacking catalytic activity, possess the ability to disrupt biological membranes, inducing significant muscle-tissue loss and permanent disability in severely envenomed patients. Since the structural basis for their toxic activity is still only partially understood, the structure of myotoxin II, a monomeric Lys49 PLA2 homologue from Atropoides nummifer, has been determined at 2.08 Å resolution and the anion-binding site has been characterized. © 2006 International Union of Crystallography. All rights reserved.en
dc.description.affiliationDepartment of Physics IBILCE/UNESP, Sao Jose do Rio Preto-SP
dc.description.affiliationInstituto Clodomiro Picado Facultad de Microbiologia, San José
dc.description.affiliationDepartamento de Bioqúmica Escuela de Medicina Universidad de Costa Rica, San José
dc.description.affiliationCenter for Applied Toxinology Butantan Institute, São Paulo-SP
dc.description.affiliationUnespDepartment of Physics IBILCE/UNESP, Sao Jose do Rio Preto-SP
dc.format.extent423-426
dc.identifierhttp://dx.doi.org/10.1107/S1744309106010700
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/16682766
dc.identifier.citationActa Crystallographica Section F: Structural Biology and Crystallization Communications, v. 62, n. 5, p. 423-426, 2006.
dc.identifier.doi10.1107/S1744309106010700
dc.identifier.doihttp://www.ncbi.nlm.nih.gov/pubmed/16682766
dc.identifier.fileWOS000237159000001.pdf
dc.identifier.issn1744-3091
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.scopus2-s2.0-33646836252
dc.identifier.urihttp://hdl.handle.net/11449/68864
dc.identifier.wosWOS:000237159000001
dc.language.isoeng
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communications
dc.rights.accessRightsAcesso aberto
dc.sourceScopus
dc.subjectAtropoides nummifer
dc.subjectmyotoxin II, Atropoides nummifer
dc.subjectphospholipase A
dc.subjectsnake venom
dc.subjectamino acid sequence
dc.subjectbinding site
dc.subjectchemistry
dc.subjectcrystallization
dc.subjectmolecular genetics
dc.subjectsequence alignment
dc.subjectX ray crystallography
dc.subjectAmino Acid Sequence
dc.subjectBinding Sites
dc.subjectCrotalid Venoms
dc.subjectCrystallization
dc.subjectCrystallography, X-Ray
dc.subjectMolecular Sequence Data
dc.subjectPhospholipases A
dc.subjectSequence Alignment
dc.titleStructure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venomen
dc.typeArtigo
dcterms.licensehttp://journals.iucr.org/services/copyrightpolicy.html
unesp.author.lattes9162508978945887[5]
unesp.author.orcid0000-0003-2460-1145[5]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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