3bmp
From Proteopedia
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| - | [[Image:3bmp.gif|left|200px]] | + | [[Image:3bmp.gif|left|200px]] |
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| - | '''HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)''' | + | {{Structure |
| + | |PDB= 3bmp |SIZE=350|CAPTION= <scene name='initialview01'>3bmp</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3BMP is a [ | + | 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]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tgfb-family]] | [[Category: tgfb-family]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:00:02 2008'' |
Revision as of 17:00, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)
Contents |
Overview
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.
Disease
Known diseases associated with this structure: HFE hemochromatosis, modifier of OMIM:[112261]
About this Structure
3BMP is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2BMP. Full crystallographic information is available from OCA.
Reference
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
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