Crytallization 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.contributorUniversidade de São Paulo (USP)
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:29:06Z
dc.date.available2014-05-20T15:29:06Z
dc.date.created2014-05-20T15:29:06Z
dc.date.issued2004-12-01
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.identifier10.1016/j.bbapap.2004.08.008
dc.identifierWOS:000225621800009
dc.identifier9162508978945887
dc.identifier0000-0003-2460-1145
dc.description.abstractSnake 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.relation2.609
dc.relation1,170
dc.rightsAcesso restrito
dc.sourceWeb of Science
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.typeArtículos de revistas


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