1ri9
From Proteopedia
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'''Structure of a helically extended SH3 domain of the T cell adapter protein ADAP''' | '''Structure of a helically extended SH3 domain of the T cell adapter protein ADAP''' | ||
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[[Category: Langdon, G.]] | [[Category: Langdon, G.]] | ||
[[Category: Thiemke, K.]] | [[Category: Thiemke, K.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:31:51 2008'' | |
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Revision as of 04:31, 3 May 2008
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 Page seeded by OCA on Sat May 3 07:31:51 2008
