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ABSTRACT: Background
Snake venom metalloproteinases (SVMPs) are widely distributed in snake venoms and are versatile toxins, targeting many important elements involved in hemostasis, such as basement membrane proteins, clotting proteins, platelets, endothelial and inflammatory cells. The functional diversity of SVMPs is in part due to the structural organization of different combinations of catalytic, disintegrin, disintegrin-like and cysteine-rich domains, which categorizes SVMPs in 3 classes of precursor molecules (PI, PII and PIII) further divided in 11 subclasses, 6 of them belonging to PII group. This heterogeneity is currently correlated to genetic accelerated evolution and post-translational modifications.Results
Thirty-one SVMP cDNAs were full length cloned from a single spec
SUBMITTER: Moura-da-Silva AM
PROVIDER: S-EPMC3217872 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature