1rew

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[[Image:1rew.gif|left|200px]]
[[Image:1rew.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1rew |SIZE=350|CAPTION= <scene name='initialview01'>1rew</scene>, resolution 1.863&Aring;
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The line below this paragraph, containing "STRUCTURE_1rew", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span>
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_1rew| PDB=1rew | SCENE= }}
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|RELATEDENTRY=[[3bmp|3BMP]], [[1es7|1ES7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rew OCA], [http://www.ebi.ac.uk/pdbsum/1rew PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rew RCSB]</span>
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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'''
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[[Category: Zhang, J L.]]
[[Category: Zhang, J L.]]
[[Category: 3-finger toxin fold]]
[[Category: 3-finger toxin fold]]
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[[Category: bria-fold]]
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[[Category: Bria-fold]]
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[[Category: tgf-beta fold]]
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[[Category: Tgf-beta fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:24:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:27:11 2008''
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Revision as of 04:24, 3 May 2008

Image:1rew.gif

Template:STRUCTURE 1rew

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


Overview

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.

About this Structure

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

Reference

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 Sat May 3 07:24:35 2008

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