1rew: Difference between revisions

Revision as of 05:52, 28 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:1rew.png

Template:STRUCTURE 1rew

Structural refinement of the complex of bone morphogenetic protein 2 and its type IA receptorStructural refinement of the complex of bone morphogenetic protein 2 and its type IA receptor

Template:ABSTRACT PUBMED 15064755

About this StructureAbout this Structure

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

ReferenceReference

Molecular recognition of BMP-2 and BMP receptor IA., Keller S, Nickel J, Zhang JL, Sebald W, Mueller TD, Nat Struct Mol Biol. 2004 May;11(5):481-8. Epub 2004 Apr 4. PMID:15064755

Page seeded by OCA on Mon Jul 28 05:52:30 2008

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OCA

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-'''Structural refinement of the complex of bone morphogenetic protein 2 and its type IA receptor'''
+===Structural refinement of the complex of bone morphogenetic protein 2 and its type IA receptor===
-==Overview==
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-Bone morphogenetic protein-2 (BMP-2) and other members of the TGF-beta superfamily regulate the development, maintenance and regeneration of tissues and organs. Binding epitopes for these extracellular signaling proteins have been defined, but hot spots specifying binding affinity and specificity have so far not been identified. In this study, mutational and structural analyses show that epitopes of BMP-2 and the BRIA receptor form a new type of protein-protein interface. The main chain atoms of Leu 51 and Asp53 of BMP-2 represent a hot spot of binding to BRIA. The BMP-2 variant L51P was deficient in type I receptor binding only, whereas its overall structure and its binding to type II receptors and modulator proteins, such as noggin, were unchanged. Thus, the L51P substitution converts BMP-2 into a receptor-inactive inhibitor of noggin. These results are relevant for other proteins of the TGF-beta superfamily and provide useful clues for structure-based drug design.
+The line below this paragraph, {{ABSTRACT_PUBMED_15064755}}, adds the Publication Abstract to the page
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