PMID- 15062083 OWN - NLM STAT- MEDLINE DCOM- 20041124 LR - 20190826 IS - 0969-2126 (Print) IS - 0969-2126 (Linking) VI - 12 IP - 4 DP - 2004 Apr TI - Structure of a helically extended SH3 domain of the T cell adapter protein ADAP. PG - 603-10 AB - 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. FAU - Heuer, Katja AU - Heuer K AD - Protein Engineering Group, Forschungsinstitut fur Molekulare Pharmakologie and Freie Universitat Berlin, Robert-Rossle-Strasse 10, 13125 Berlin, Germany. FAU - Kofler, Michael AU - Kofler M FAU - Langdon, Grant AU - Langdon G FAU - Thiemke, Katharina AU - Thiemke K FAU - Freund, Christian AU - Freund C LA - eng SI - PDB/1RI9 PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - United States TA - Structure JT - Structure (London, England : 1993) JID - 101087697 RN - 0 (Adaptor Proteins, Signal Transducing) RN - 0 (FYB1 protein, human) SB - IM MH - Adaptor Proteins, Signal Transducing/*chemistry/metabolism MH - Amino Acid Sequence MH - Cell Adhesion/physiology MH - Humans MH - Magnetic Resonance Spectroscopy MH - Molecular Sequence Data MH - Protein Structure, Tertiary MH - T-Lymphocytes/metabolism EDAT- 2004/04/06 05:00 MHDA- 2004/12/16 09:00 CRDT- 2004/04/06 05:00 PHST- 2003/11/14 00:00 [received] PHST- 2004/01/12 00:00 [revised] PHST- 2004/01/12 00:00 [accepted] PHST- 2004/04/06 05:00 [pubmed] PHST- 2004/12/16 09:00 [medline] PHST- 2004/04/06 05:00 [entrez] AID - S0969212604000632 [pii] AID - 10.1016/j.str.2004.02.021 [doi] PST - ppublish SO - Structure. 2004 Apr;12(4):603-10. doi: 10.1016/j.str.2004.02.021.