Murakami, Mário T. [UNESP]Melo, Cristiane C. [UNESP]Angulo, YamilethLomonte, BrunoArni, Raghuvir K. [UNESP]2014-05-272014-05-272006-05-01Acta Crystallographica Section F: Structural Biology and Crystallization Communications, v. 62, n. 5, p. 423-426, 2006.1744-3091http://hdl.handle.net/11449/68864Lys49 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.423-426engAtropoides nummifermyotoxin II, Atropoides nummiferphospholipase Asnake venomamino acid sequencebinding sitechemistrycrystallizationmolecular geneticssequence alignmentX ray crystallographyAmino Acid SequenceBinding SitesCrotalid VenomsCrystallizationCrystallography, X-RayMolecular Sequence DataPhospholipases ASequence AlignmentArtigo10.1107/S1744309106010700http://www.ncbi.nlm.nih.gov/pubmed/16682766WOS:000237159000001Acesso aberto2-s2.0-33646836252WOS000237159000001.pdf91625089789458870000-0003-2460-1145