3bk3

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Revision as of 06:19, 28 May 2008

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Template:STRUCTURE 3bk3

Crystal structure of the complex of BMP-2 and the first Von Willebrand domain type C of Crossveinless-2

Overview

Crossveinless 2 (CV-2) is an extracellular BMP modulator protein belonging to the Chordin family. During development it is expressed at sites of high BMP signaling and like Chordin CV-2 can either enhance or inhibit BMP activity. CV-2 binds to BMP-2 via its N-terminal Von Willebrand factor type C (VWC) domain 1. Here we report the structure of the complex between CV-2 VWC1 and BMP-2. The tripartite VWC1 binds BMP-2 only through a short N-terminal segment, called clip, and subdomain (SD) 1. Mutational analysis establishes that the clip segment and SD1 together create high-affinity BMP-2 binding. All four receptor-binding sites of BMP-2 are blocked in the complex, demonstrating that VWC1 acts as competitive inhibitor for all receptor types. In vivo experiments reveal that the BMP-enhancing (pro-BMP) activity of CV-2 is independent of BMP-2 binding by VWC1, showing that pro- and anti-BMP activities are structurally separated in CV-2.

About this Structure

3BK3 is a Protein complex structure of sequences from Danio rerio and Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure analysis reveals how the Chordin family member crossveinless 2 blocks BMP-2 receptor binding., Zhang JL, Qiu LY, Kotzsch A, Weidauer S, Patterson L, Hammerschmidt M, Sebald W, Mueller TD, Dev Cell. 2008 May;14(5):739-50. PMID:18477456 Page seeded by OCA on Wed May 28 09:19:23 2008