dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorMurakami, M. T.
dc.creatorMichelan-Duarte, S.
dc.creatorCintra, ACO
dc.creatorArni, R. K.
dc.date2014-05-20T15:29:06Z
dc.date2016-10-25T18:04:18Z
dc.date2014-05-20T15:29:06Z
dc.date2016-10-25T18:04:18Z
dc.date2004-12-01
dc.date.accessioned2017-04-06T00:10:25Z
dc.date.available2017-04-06T00:10:25Z
dc.identifierBiochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1703, n. 1, p. 79-81, 2004.
dc.identifier1570-9639
dc.identifierhttp://hdl.handle.net/11449/38760
dc.identifierhttp://acervodigital.unesp.br/handle/11449/38760
dc.identifier10.1016/j.bbapap.2004.08.008
dc.identifierWOS:000225621800009
dc.identifierhttp://dx.doi.org/10.1016/j.bbapap.2004.08.008
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/881811
dc.descriptionSnake venom PLA(2)s have been extensively studied due to their role in mediating and disrupting physiological processes such as coagulation, platelet aggregation and myotoxicity. The Ca2+ ion bound to the putative calcium-binding loop is essential for hydrolytic activity. We report the crystallization in the presence and absence of Ca2+ and X-ray diffraction data collection at 1.60 Angstrom (with Ca2+) and 1.36 Angstrom (without Ca2+) of an Asp49 PLA(2) from Bothrops jararacussu venom. The crystals belong to orthorhombic space group C222(1). Initial refinement and electron density analysis indicate significant conformational. changes upon Ca2+ binding. (C) 2004 Elsevier B.V. All fights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBiochimica et Biophysica Acta: Proteins and Proteomics
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectcalcium-binding loop
dc.subjectAsp49 PLA(2)
dc.subjectcrystallization
dc.subjectX-ray diffraction
dc.titleCrytallization and high-resolution X-ray diffraction data collection of an Asp49 PLA(2) from Bothrops jararacussu venom both in the presence and absence of Ca2+ ions
dc.typeOtro


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