1es7: Difference between revisions

Revision as of 01:47, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1es7.png

Template:STRUCTURE 1es7

COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINSCOMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS

Template:ABSTRACT PUBMED 10881198

About this StructureAbout this Structure

1ES7 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the BMP-2-BRIA ectodomain complex., Kirsch T, Sebald W, Dreyer MK, Nat Struct Biol. 2000 Jun;7(6):492-6. PMID:10881198

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+===COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS===
-==Overview==
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-Bone morphogenetic proteins (BMPs) belong to the large transforming growth factor-beta (TGF-beta) superfamily of multifunctional cytokines. BMP-2 can induce ectopic bone and cartilage formation in adult vertebrates and is involved in central steps in early embryonal development in animals. Signaling by these cytokines requires binding of two types of transmembrane serine/threonine receptor kinase chains classified as type I and type II. Here we report the crystal structure of human dimeric BMP-2 in complex with two high affinity BMP receptor IA extracellular domains (BRIAec). The receptor chains bind to the 'wrist' epitopes of the BMP-2 dimer and contact both BMP-2 monomers. No contacts exist between the receptor domains. The model reveals the structural basis for discrimination between type I and type II receptors and the variability of receptor-ligand interactions that is seen in BMP-TGF-beta systems.
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