Crystal Structures of Catrocollastatin/VAP2B Reveal a Dynamic, Modular Architecture of ADAM/adamalysin/reprolysin Family Proteins

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 2007 May 9

PMID 17485084

Citations 37

Authors

Tomoko Igarashi

Satohiko Araki

Hidezo Mori

Soichi Takeda

Affiliations

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Abstract

Catrocollastatin/vascular apoptosis-inducing protein (VAP)2B is a metalloproteinase from Crotalus atrox venom, possessing metalloproteinase/disintegrin/cysteine-rich (MDC) domains that bear the typical domain architecture of a disintegrin and metalloproteinase (ADAM)/adamalysin/reprolysin family proteins. Here we describe crystal structures of catrocollastatin/VAP2B in three different crystal forms, representing the first reported crystal structures of a member of the monomeric class of this family of proteins. The overall structures show good agreement with both monomers of atypical homodimeric VAP1. Comparison of the six catrocollastatin/VAP2B monomer structures and the structures of VAP1 reveals a dynamic, modular architecture that may be important for the functions of ADAM/adamalysin/reprolysin family proteins.

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