Journal
FEBS LETTERS
Volume 581, Issue 30, Pages 5859-5864Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.11.062
Keywords
metalloproteinase; disintegrin; ADAM; factor X activator; snake venom; reprolysin
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Russell's viper venom factor X activator (RVV-X) is a heterotrimeric metalloproteinase with a mammalian ADAM-like heavy chain and two lectin-like light chains. The crystal structure of RVV-X has been determined at 2.9 angstrom resolution and shows a hook-spanner-wrench-like architecture, in which the metalloproteinase/disintegrin region constitutes a hook, and the lectin-like domains constitute a handle. A 6.5 nm separation between the catalytic site and a putative exosite suggests a docking model for factor X. The structure provides a typical example of the molecular evolution of multi-subunit proteins and insights into the molecular basis of target recognition and proteolysis by ADAM/adamalysin/reprolysin proteinases. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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