dc.creatorMurakami, Mário T.
dc.creatorMelo, Cristiane C.
dc.creatorAngulo Ugalde, Yamileth
dc.creatorLomonte, Bruno
dc.creatorArni, Raghuvir K.
dc.date.accessioned2018-02-26T21:26:31Z
dc.date.accessioned2022-10-20T00:05:44Z
dc.date.available2018-02-26T21:26:31Z
dc.date.available2022-10-20T00:05:44Z
dc.date.created2018-02-26T21:26:31Z
dc.date.issued2006
dc.identifierhttp://scripts.iucr.org/cgi-bin/paper?S1744309106010700
dc.identifier1744-3091
dc.identifierhttps://hdl.handle.net/10669/74162
dc.identifier10.1107/S1744309106010700
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4528827
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 A ° resolution and the anion-binding site has been characterized.
dc.languageen_US
dc.sourceActa Crystallographica F 62, 423-426 (2006)
dc.subjectmyotoxin
dc.subjectSnake venom
dc.subjectLys49 phospholipase A2
dc.subjectanion-binding sites
dc.titleStructure of myotoxin-II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
dc.typeartículo científico


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