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| | <StructureSection load='3bmp' size='340' side='right'caption='[[3bmp]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='3bmp' size='340' side='right'caption='[[3bmp]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3bmp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BMP FirstGlance]. <br> | + | <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> |
| - | </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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=3bmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bmp OCA], [http://pdbe.org/3bmp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bmp RCSB], [http://www.ebi.ac.uk/pdbsum/3bmp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bmp ProSAT]</span></td></tr> | + | <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> |
| | + | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BMP2_HUMAN BMP2_HUMAN]] Induces cartilage and bone formation. | + | [https://www.uniprot.org/uniprot/BMP2_HUMAN BMP2_HUMAN] Induces cartilage and bone formation. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Huelsmeyer, M]] | + | [[Category: Huelsmeyer M]] |
| - | [[Category: Scheufler, C]] | + | [[Category: Scheufler C]] |
| - | [[Category: Sebald, W]] | + | [[Category: Sebald W]] |
| - | [[Category: Bone morphogenetic protein]]
| + | |
| - | [[Category: Cystin-knot]]
| + | |
| - | [[Category: Cytokine]]
| + | |
| - | [[Category: Tgfb-family]]
| + | |
| 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 PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Scheufler C, Sebald W, Hulsmeyer M. Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution. J Mol Biol. 1999 Mar 19;287(1):103-15. PMID:10074410 doi:10.1006/jmbi.1999.2590
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