1ri9
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(New page: 200px<br /> <applet load="1ri9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ri9" /> '''Structure of a helically extended SH3 domai...)
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Revision as of 16:57, 12 November 2007
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Structure of a helically extended SH3 domain of the T cell adapter protein ADAP
Overview
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.
About this Structure
1RI9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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