3bmp

HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)

spinqualitylabelsall models 3bmp, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3bmp is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2bmp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bone morphogenetic protein 3D structures

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