1ri9 Citations

Structure of a helically extended SH3 domain of the T cell adapter protein ADAP.

Structure 12 603-10 (2004)
Cited: 10 times
EuropePMC logo PMID: 15062083

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.

Reviews citing this publication (4)

  1. T-cell receptor signaling to integrins. Burbach BJ, Medeiros RB, Mueller KL, Shimizu Y. Immunol. Rev. 218 65-81 (2007)
  2. Regulation of T-cell antigen receptor-mediated inside-out signaling by cytosolic adapter proteins and Rap1 effector molecules. Ménasché G, Kliche S, Bezman N, Schraven B. Immunol. Rev. 218 82-91 (2007)
  3. T-cell receptor signaling to integrins. Burbach BJ, Medeiros RB, Mueller KL, Shimizu Y. Immunol. Rev. 218 65-81 (2007)
  4. Regulation of T-cell antigen receptor-mediated inside-out signaling by cytosolic adapter proteins and Rap1 effector molecules. Ménasché G, Kliche S, Bezman N, Schraven B. Immunol. Rev. 218 82-91 (2007)

Articles citing this publication (6)

  1. Protein structure database search and evolutionary classification. Yang JM, Tung CH. Nucleic Acids Res. 34 3646-3659 (2006)
  2. Adhesion and degranulation promoting adapter protein (ADAP) is a central hub for phosphotyrosine-mediated interactions in T cells. Sylvester M, Kliche S, Lange S, Geithner S, Klemm C, Schlosser A, Grossmann A, Stelzl U, Schraven B, Krause E, Freund C. PLoS ONE 5 e11708 (2010)
  3. A novel S3S-TAP-tag for the isolation of T-cell interaction partners of adhesion and degranulation promoting adaptor protein. Lehmann R, Meyer J, Schuemann M, Krause E, Freund C. Proteomics 9 5288-5295 (2009)
  4. Phosphorylation of Ser-180 of rat aquaporin-4 shows marginal affect on regulation of water permeability: molecular dynamics study. Sachdeva R, Singh B. J. Biomol. Struct. Dyn. 32 555-566 (2014)
  5. A novel hSH3 domain scaffold engineered to bind folded domains in CD2BP2 and HIV capsid protein. Piotukh K, Freund C. Protein Eng. Des. Sel. 25 649-656 (2012)
  6. Tyrosine-phosphorylation of the scaffold protein ADAP and its role in T cell signaling. Kuropka B, Schraven B, Kliche S, Krause E, Freund C. Expert Rev Proteomics 13 545-554 (2016)