5ABS
CRYSTAL STRUCTURE OF THE C-TERMINAL COILED-COIL DOMAIN OF CIN85 IN SPACE GROUP P321
Summary for 5ABS
| Entry DOI | 10.2210/pdb5abs/pdb |
| Related | 2N64 |
| Descriptor | SH3 DOMAIN-CONTAINING KINASE-BINDING PROTEIN 1, ZINC ION (3 entities in total) |
| Functional Keywords | signaling protein, cbl-interacting protein of 85 kda, adapter protein, coiled-coil domain, b-cell antigen receptor signaling |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 8147.29 |
| Authors | Wong, L.,Habeck, M.,Griesinger, C.,Becker, S. (deposition date: 2015-08-07, release date: 2016-07-13, Last modification date: 2024-11-06) |
| Primary citation | Kuhn, J.,Wong, L.E.,Pirkuliyeva, S.,Schulz, K.,Schwiegk, C.,Funfgeld, K.G.,Keppler, S.,Batista, F.D.,Urlaub, H.,Habeck, M.,Becker, S.,Griesinger, C.,Wienands, J. The Adaptor Protein Cin85 Assembles Intracellular Signaling Clusters for B Cell Activation. Sci.Signal., 9:RA66-, 2016 Cited by PubMed Abstract: The adaptor molecule Cbl-interacting protein of 85 kD (CIN85) regulates signaling from a number of cell surface receptors, such as growth factor receptors and antigen receptors on lymphocytes. Because of its multidomain structure, CIN85 is thought to act as a classical adaptor protein that connects functionally distinct components of a given signaling pathway through diverse protein domains. However, we found that in B lymphocytes, CIN85 functions to oligomerize SLP-65, which is the central effector protein of the B cell receptor (BCR). Therefore, CIN85 trimerizes through a carboxyl-terminal, coiled-coil domain. The multiple Src homology 3 (SH3) domains of trimeric CIN85 molecules associated with multiple SLP-65 molecules, which recruited further CIN85 trimers, thereby perpetuating the oligomerization process. Formation of this oligomeric signaling complex in resting B cells rendered the cells poised for the efficient initiation of intracellular signaling upon BCR stimulation. Our data suggest that the functionality of signaling cascades does not rely solely on the qualitative linkage of their various components but requires a critical number of effectors to become concentrated in signaling complexes. PubMed: 27353366DOI: 10.1126/SCISIGNAL.AAD6275 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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