2K3G
NMR structure analysis of a BMP receptor
Summary for 2K3G
| Entry DOI | 10.2210/pdb2k3g/pdb |
| NMR Information | BMRB: 15956 |
| Descriptor | Bone morphogenetic protein receptor type-1A (1 entity in total) |
| Functional Keywords | bmp, receptor, tgf-beta superfamily, atp-binding, disease mutation, glycoprotein, kinase, magnesium, manganese, membrane, metal-binding, nucleotide-binding, phosphoprotein, polymorphism, serine/threonine-protein kinase, transferase, transmembrane, signaling protein |
| Biological source | Homo sapiens |
| Cellular location | Membrane; Single-pass type I membrane protein: P36894 |
| Total number of polymer chains | 1 |
| Total formula weight | 11278.69 |
| Authors | Klages, J.,Kotzsch, A.,Mueller, T.,Kessler, H. (deposition date: 2008-05-07, release date: 2008-12-16, Last modification date: 2024-10-30) |
| Primary citation | Klages, J.,Kotzsch, A.,Coles, M.,Sebald, W.,Nickel, J.,Muller, T.,Kessler, H. The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding. Biochemistry, 47:11930-11939, 2008 Cited by PubMed Abstract: The structure of the extracellular domain of BMP receptor IA was determined in solution by NMR spectroscopy and compared to its structure when bound to its ligand BMP-2. While most parts of the secondary structure are highly conserved between the bound and unbound forms, large conformational rearrangements can be observed in the beta4beta5 loop of BMPR-IA, which is in contact with BMP-2 and harbors the main binding determinants for the BMPR-IA-BMP-2 interaction. In its unbound form, helix alpha1 in BMPR-IA, which is in the center of the binding epitope for BMP-2, is missing. Since BMP-2 also shows conformational changes in the type I receptor epitope upon binding to BMPR-IA, both binding partners pass through an induced fit mechanism to adapt their binding interfaces to a given interaction surface. The inherent flexibility of both partners possibly explains the promiscuous ligand-receptor interaction observed in the BMP protein superfamily. PubMed: 18937504DOI: 10.1021/bi801059j PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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