1B0X
THE CRYSTAL STRUCTURE OF AN EPH RECEPTOR SAM DOMAIN REVEALS A MECHANISM FOR MODULAR DIMERIZATION.
Summary for 1B0X
| Entry DOI | 10.2210/pdb1b0x/pdb |
| Descriptor | PROTEIN (EPHA4 RECEPTOR TYROSINE KINASE) (2 entities in total) |
| Functional Keywords | receptor tyrosine kinase, protein interaction module, dimerization domain, transferase |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Membrane; Single-pass type I membrane protein: Q03137 |
| Total number of polymer chains | 1 |
| Total formula weight | 10265.49 |
| Authors | Stapleton, D.,Balan, I.,Pawson, T.,Sicheri, F. (deposition date: 1998-11-14, release date: 1999-05-03, Last modification date: 2023-12-27) |
| Primary citation | Stapleton, D.,Balan, I.,Pawson, T.,Sicheri, F. The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization. Nat.Struct.Biol., 6:44-49, 1999 Cited by PubMed Abstract: The sterile alpha motif (SAM) domain is a novel protein module of approximately 70 amino acids that is found in a variety of signaling molecules including tyrosine and serine/threonine protein kinases, cytoplasmic scaffolding and adaptor proteins, regulators of lipid metabolism, and GTPases as well as members of the ETS family of transcription factors. The SAM domain can potentially function as a protein interaction module through the ability to homo- and hetero-oligomerize with other SAM domains. This functional property elicits the oncogenic activation of chimeric proteins arising from translocation of the SAM domain of TEL to coding regions of the betaPDGF receptor, Abl, JAK2 protein kinase and the AML1 transcription factor. Here we describe the 2.0 A X-ray crystal structure of a SAM domain homodimer from the intracellular region of the EphA4 receptor tyrosine kinase. The structure reveals a mode of dimerization that we predict is shared amongst the SAM domains of the Eph receptor tyrosine kinases and possibly other SAM domain containing proteins. These data indicate a mechanism through which an independently folding protein module can form homophilic complexes that regulate signaling events at the membrane and in the nucleus. PubMed: 9886291DOI: 10.1038/4917 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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