3bmp
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(New page: 200px<br /> <applet load="3bmp" size="450" color="white" frame="true" align="right" spinBox="true" caption="3bmp, resolution 2.7Å" /> '''HUMAN BONE MORPHOGEN...)
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Revision as of 21:41, 12 November 2007
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HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)
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.
About this Structure
3BMP is a Single protein structure of sequence from Homo sapiens with MPD as ligand. This structure superseeds 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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