1RI9

Structure of a Helically Extended SH3 Domain of the T Cell Adapter Protein ADAP.

(2004) Structure 12: 603-610

• PubMed: 15062083 Search on PubMed
• DOI: https://doi.org/10.1016/j.str.2004.02.021
• Primary Citation of Related Structures:  
  1RI9


• PubMed Abstract: 
  

  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.

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Organizational Affiliation: 

Protein Engineering Group, Forschungsinstitut für Molekulare Pharmakologie and Freie Universität Berlin, Robert-Rössle-Strasse 10, 13125 Berlin, Germany.