biostudies-literatureNishizawa KNIAID NIH HHS14897-902https://www.ebi.ac.uk/biostudies/studies/S-EPMC24547biostudies-literatureUnknown95(25)An intracellular protein termed CD2 binding protein 2 (CD2BP2), which binds to a site containing two PPPGHR segments within the cytoplasmic region of CD2, was identified. Mutagenesis and NMR analysis demonstrated that the CD2 binding region of CD2BP2 includes a 17-aa motif (GPY[orF]xxxxM[orV]xxWxxx GYF), also found in several yeast and Caenorhabditis elegans proteins of unknown function. In Jurkat T cells, over-expression of the isolated CD2BP2 domain binding to CD2 enhances the production of interleukin 2 on crosslinking of CD2 but not the T cell receptor. Hence, a proline-binding module distinct from SH3 and WW domains regulates protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of AmericaIdentification of a proline-binding motif regulating CD2-triggered T lymphocyte activation.PMC24547AI27581AI21226Freund CLi JNishizawa KWagner GReinherz ELfalseIdentification of a proline-binding motif regulating CD2-triggered T lymphocyte activation.An intracellular protein termed CD2 binding protein 2 (CD2BP2), which binds to a site containing two PPPGHR segments within the cytoplasmic region of CD2, was identified. Mutagenesis and NMR analysis demonstrated that the CD2 binding region of CD2BP2 includes a 17-aa motif (GPY[orF]xxxxM[orV]xxWxxx GYF), also found in several yeast and Caenorhabditis elegans proteins of unknown function. In Jurkat T cells, over-expression of the isolated CD2BP2 domain binding to CD2 enhances the production of interleukin 2 on crosslinking of CD2 but not the T cell receptor. Hence, a proline-binding module distinct from SH3 and WW domains regulates protein-protein interactions.1998-01-01T00:00:00Z1998 Dec2025-04-26T23:39:08.441Z2019-03-27T00:17:52ZS-EPMC24547984398710.1073/pnas.95.25.14897