1RI9

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

Summary for 1RI9

• Entry DOI: 10.2210/pdb1ri9/pdb
• NMR Information: BMRB: 5467
• Descriptor: FYN-binding protein (1 entity in total)
• Functional Keywords: sh3-like, helically extended, signaling protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 11901.39

Authors

Heuer, K.,Kofler, M.,Langdon, G.,Thiemke, K.,Freund, C. (deposition date: 2003-11-17, release date: 2004-04-20, Last modification date: 2024-05-08)

Primary citation

Heuer, K.,Kofler, M.,Langdon, G.,Thiemke, K.,Freund, C.
Structure of a Helically Extended SH3 Domain of the T Cell Adapter Protein ADAP.
STRUCTURE, 12:603-610, 2004

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.

PubMed: 15062083
DOI: 10.1016/j.str.2004.02.021

Experimental method

SOLUTION NMR