1ri9
From Proteopedia
Structure of a helically extended SH3 domain of the T cell adapter protein ADAP
Structural highlights
DiseaseFYB1_HUMAN Congenital autosomal recessive small-platelet thrombocytopenia. The disease is caused by variants affecting the gene represented in this entry. FunctionFYB1_HUMAN Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (PubMed:10747096, PubMed:16980616). Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity). Prevents the degradation of SKAP1 and SKAP2 (PubMed:15849195). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity).[UniProtKB:D3ZIE4][UniProtKB:O35601][1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe adapter protein ADAP (FYB/SLAP-130) provides a critical link between T cell receptor (TCR) signaling and cell adhesion via the activation of integrins. The C-terminal 70 residues of ADAP show homology to SH3 domains; however, conserved residues of the fold are absent. An alignment and annotation of this domain has therefore been elusive. We have solved the three-dimensional structure of the ADAP C-terminal domain by NMR spectroscopy and show that it represents an altered SH3 domain fold. An N-terminal, amphipathic helix makes extensive contacts to residues of the regular SH3 domain fold, and thereby a composite surface with unusual surface properties is created. We propose this SH3 domain variant to be classified as a helically extended SH3 domain (hSH3 domain) and show that the ADAP-hSH3 domain can no longer bind conventional proline-rich peptides. Structure of a helically extended SH3 domain of the T cell adapter protein ADAP.,Heuer K, Kofler M, Langdon G, Thiemke K, Freund C Structure. 2004 Apr;12(4):603-10. PMID:15062083[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Homo sapiens | Large Structures | Freund C | Heuer K | Kofler M | Langdon G | Thiemke K
