3bmp: Difference between revisions
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New page: left|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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[[Image:3bmp.gif|left|200px]]<br /> | [[Image:3bmp.gif|left|200px]]<br /><applet load="3bmp" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="3bmp" size=" | |||
caption="3bmp, resolution 2.7Å" /> | caption="3bmp, resolution 2.7Å" /> | ||
'''HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)'''<br /> | '''HUMAN BONE MORPHOGENETIC PROTEIN-2 (BMP-2)'''<br /> | ||
==Overview== | ==Overview== | ||
Homodimeric bone morphogenetic protein-2 (BMP-2) is a member of the | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=112261 112261]] | |||
==About this Structure== | ==About this Structure== | ||
3BMP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MPD as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | 3BMP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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== | ||
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[[Category: tgfb-family]] | [[Category: tgfb-family]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:06:37 2008'' | ||