1ri9 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Heuer K, Kofler M, Langdon G, Thiemke K, Freund C. Structure of a helically extended SH3 domain of the T cell adapter protein ADAP. Structure. 2004 Apr;12(4):603-10. PMID:15062083 doi:10.1016/j.str.2004.02.021
