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3bmp

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[[Image:3bmp.gif|left|200px]]
 
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{{Structure
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==HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)==
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|PDB= 3bmp |SIZE=350|CAPTION= <scene name='initialview01'>3bmp</scene>, resolution 2.7&Aring;
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<StructureSection load='3bmp' size='340' side='right'caption='[[3bmp]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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<table><tr><td colspan='2'>[[3bmp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bmp 2bmp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BMP FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bmp OCA], [https://pdbe.org/3bmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bmp RCSB], [https://www.ebi.ac.uk/pdbsum/3bmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bmp ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bmp OCA], [http://www.ebi.ac.uk/pdbsum/3bmp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bmp RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/BMP2_HUMAN BMP2_HUMAN] Induces cartilage and bone formation.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/3bmp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bmp ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Homodimeric bone morphogenetic protein-2 (BMP-2) is a member of the transforming growth factor beta (TGF-beta) superfamily that induces bone formation and regeneration, and determines important steps during early stages of embryonic development in vertebrates and non-vertebrates. BMP-2 can interact with two types of receptor chains, as well as with proteins of the extracellular matrix and several regulatory proteins. We report here the crystal structure of human BMP-2 determined by molecular replacement and refined to an R-value of 24.2 % at 2.7 A resolution. A common scaffold of BMP-2, BMP-7 and the TGF-betas, i.e. the cystine-knot motif and two finger-like double-stranded beta-sheets, can be superimposed with r. m.s. deviations of around 1 A. In contrast to the TGF-betas, the structure of BMP-2 shows differences in the flexibility of the N terminus and the orientation of the central alpha-helix as well as two external loops at the fingertips with respect to the scaffold. This is also known from the BMP-7 model. Small secondary structure elements in the loop regions of BMP-2 and BMP-7 seem to be specific for the respective BMP-subgroup. Two identical helix-finger clefts and two distinct cavities located around the central 2-fold axis of the dimer show characteristic shapes, polarity and surface charges. The possible function of these specific features in the interaction of BMP-2 with its binding partners is discussed.
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'''HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)'''
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Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution.,Scheufler C, Sebald W, Hulsmeyer M J Mol Biol. 1999 Mar 19;287(1):103-15. PMID:10074410<ref>PMID:10074410</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3bmp" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Homodimeric bone morphogenetic protein-2 (BMP-2) is a member of the transforming growth factor beta (TGF-beta) superfamily that induces bone formation and regeneration, and determines important steps during early stages of embryonic development in vertebrates and non-vertebrates. BMP-2 can interact with two types of receptor chains, as well as with proteins of the extracellular matrix and several regulatory proteins. We report here the crystal structure of human BMP-2 determined by molecular replacement and refined to an R-value of 24.2 % at 2.7 A resolution. A common scaffold of BMP-2, BMP-7 and the TGF-betas, i.e. the cystine-knot motif and two finger-like double-stranded beta-sheets, can be superimposed with r. m.s. deviations of around 1 A. In contrast to the TGF-betas, the structure of BMP-2 shows differences in the flexibility of the N terminus and the orientation of the central alpha-helix as well as two external loops at the fingertips with respect to the scaffold. This is also known from the BMP-7 model. Small secondary structure elements in the loop regions of BMP-2 and BMP-7 seem to be specific for the respective BMP-subgroup. Two identical helix-finger clefts and two distinct cavities located around the central 2-fold axis of the dimer show characteristic shapes, polarity and surface charges. The possible function of these specific features in the interaction of BMP-2 with its binding partners is discussed.
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*[[Bone morphogenetic protein 3D structures|Bone morphogenetic protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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3BMP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 2BMP. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BMP OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution., Scheufler C, Sebald W, Hulsmeyer M, J Mol Biol. 1999 Mar 19;287(1):103-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10074410 10074410]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Huelsmeyer, M.]]
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[[Category: Huelsmeyer M]]
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[[Category: Scheufler, C.]]
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[[Category: Scheufler C]]
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[[Category: Sebald, W.]]
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[[Category: Sebald W]]
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[[Category: bone morphogenetic protein]]
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[[Category: cystin-knot]]
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[[Category: cytokine]]
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[[Category: tgfb-family]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:27:29 2008''
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Current revision

HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)

PDB ID 3bmp

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