1reu: Difference between revisions
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==Structure of the bone morphogenetic protein 2 mutant L51P== | ==Structure of the bone morphogenetic protein 2 mutant L51P== | ||
<StructureSection load='1reu' size='340' side='right' caption='[[1reu]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='1reu' size='340' side='right' caption='[[1reu]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bmp|3bmp]], [[1es7|1es7]], [[1rew|1rew]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bmp|3bmp]], [[1es7|1es7]], [[1rew|1rew]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1reu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1reu OCA], [http://pdbe.org/1reu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1reu RCSB], [http://www.ebi.ac.uk/pdbsum/1reu PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1reu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1reu OCA], [http://pdbe.org/1reu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1reu RCSB], [http://www.ebi.ac.uk/pdbsum/1reu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1reu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/1reu_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/1reu_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1reu" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1reu" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Bone morphogenetic protein|Bone morphogenetic protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:52, 28 February 2018
Structure of the bone morphogenetic protein 2 mutant L51PStructure of the bone morphogenetic protein 2 mutant L51P
Structural highlights
Function[BMP2_HUMAN] Induces cartilage and bone formation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBone 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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