Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases |
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Authors: | Takeda Soichi Igarashi Tomoko Mori Hidezo |
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Institution: | Department of Cardiac Physiology, National Cardiovascular Center Research Institute, 5-7-1 Fujishiro-dai, Suita, Osaka 565-8565, Japan. stakeda@ri.ncvc.go.jp |
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Abstract: | 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 A 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 6.5nm 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. |
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Keywords: | RVV-X Russell’s viper venom factor X activator ADAM a disintegrin and metalloproteinase MDC metalloproteinase/disintegrin/cysteine-rich HVR hyper-variable-region PEG polyethyleneglycol |
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