Summary for 3BMP
| Entry DOI | 10.2210/pdb3bmp/pdb |
| Descriptor | PROTEIN (BONE MORPHOGENETIC PROTEIN 2 (BMP-2)), (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total) |
| Functional Keywords | cytokine, bone morphogenetic protein, cystin-knot, tgfb-family |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P12643 |
| Total number of polymer chains | 1 |
| Total formula weight | 13042.03 |
| Authors | Scheufler, C.,Sebald, W.,Huelsmeyer, M. (deposition date: 1999-03-12, release date: 2000-03-12, Last modification date: 2023-08-30) |
| Primary citation | Scheufler, C.,Sebald, W.,Hulsmeyer, M. Crystal structure of human bone morphogenetic protein-2 at 2.7 A resolution. J.Mol.Biol., 287:103-115, 1999 Cited by PubMed Abstract: 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. PubMed: 10074410DOI: 10.1006/jmbi.1999.2590 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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