Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
Lys49 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 bas...
| Autores: | , , , , |
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| Formato: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2006 |
| País: | Brasil |
| Recursos: | Universidade Estadual Paulista (UNESP) |
| Repositorio: | Repositório Institucional da UNESP |
| Idioma: | inglés |
| OAI Identifier: | oai:repositorio.unesp.br:11449/68864 |
| Acesso em linha: | http://dx.doi.org/10.1107/S1744309106010700 http://www.ncbi.nlm.nih.gov/pubmed/16682766 http://hdl.handle.net/11449/68864 |
| Access Level: | acceso abierto |
| Palavra-chave: | Atropoides nummifer myotoxin II, Atropoides nummifer phospholipase A snake venom amino acid sequence binding site chemistry crystallization molecular genetics sequence alignment X ray crystallography Amino Acid Sequence Binding Sites Crotalid Venoms Crystallization Crystallography, X-Ray Molecular Sequence Data Phospholipases A Sequence Alignment |
| Resumo: | Lys49 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. |
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