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dc.creatorde Sousa, Marcelo Valle
dc.creatorMorhy, Lauro
dc.creatorArni, Raghuvir K.
dc.creatorWard, Richard John
dc.creatorDíaz Oreiro, Cecilia
dc.creatorGutiérrez, José María
dc.date.accessioned2017-01-18T17:46:01Z
dc.date.available2017-01-18T17:46:01Z
dc.date.issued1998-05-19
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S0167483898000235
dc.identifier.issn0167-4838
dc.identifier.urihttps://hdl.handle.net/10669/29436
dc.description.abstractThe complete amino acid sequence of myotoxin II (godMT-II), a myotoxic phospholipase A2 (PLA2) homologue from the venom of the Central American crotaline snake Cerrophidion (Bothrops) godmani, was determined by direct protein sequencing methods. GodMT-II is a class II PLA2 showing a Lys instead of Asp at position 49. An additional substitution in the calcium binding loop region (Asn instead of Tyr at position 28) suggests the lack of enzymatic activity observed in this toxin is due to loss of its ability to bind the co-factor Ca2+, since the residues involved in forming the catalytic network of PLA2s (His-48, Tyr-52 and Asp-99) are conserved in godMT-II. This myotoxin shows highest sequence homology with other Lys-49 PLA2 s from Bothrops, Agkistrodon and Trimeresurus species, suggesting that they constitute a conserved family of proteins, yet in contrast presents lower homology with Bothrops asper myotoxin III, a catalytically-active PLA2. The C-terminal region of godMT-II, which is rich in cationic and hydrophobic residues, shares high sequence homology to the corresponding region in the myotoxin II from B. asper, which has been proposed to play an important role in the Ca(2+)-independent membrane damaging activity.es_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-96-265]/UCR/Costa Ricaes_ES
dc.description.sponsorshipUNiversidad de Brasilia//FUB-UnB/Brasiles_ES
dc.description.sponsorshipMinistério da Ciência, Tecnologia, Inovações e Comunicações//CNPq/Brasiles_ES
dc.description.sponsorshipFundação para O Desenvolvimento da Unesp-Fundunesp//FUNDESP/Brasiles_ES
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo//FAPESP/Brasiles_ES
dc.language.isoen_USes_ES
dc.sourceBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. Volumen 1384, Número 2, 1998es_ES
dc.subjectAmino Acid Sequencees_ES
dc.subjectAnimalses_ES
dc.subjectBothropses_ES
dc.subjectCrotalid Venomses_ES
dc.subjectGroup II Phospholipases A2es_ES
dc.subjectMolecular Sequence Dataes_ES
dc.subjectNeurotoxinses_ES
dc.subjectPhospholipases Aes_ES
dc.subjectPhospholipases A2es_ES
dc.subjectReptilian Proteinses_ES
dc.subjectSequence Alignmentes_ES
dc.subjectSequence Homology, Amino Acides_ES
dc.subjectSnake venomes_ES
dc.titleAmino acid sequence of a myotoxic Lys49-phospholipase A2 homologue from the venom of Cerrophidion (Bothrops) godmanies_ES
dc.typeartículo científico
dc.identifier.doi10.1016/S0167-4838(98)00023-5es_ES
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.codproyecto741-96-265


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