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="450" color="white" frame="true" align="right" spinBox="true"  
caption="3bmp, resolution 2.7&Aring;" />
caption="3bmp, resolution 2.7&Aring;" />
'''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, 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.
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 superseeds the now removed PDB entry 2BMP. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3BMP OCA].  
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]]


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