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Can we infer peptide recognition specificity mediated by SH3 domains?
Author(s) -
Cesareni Gianni,
Panni Simona,
Nardelli Giuliano,
Castagnoli Luisa
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03307-5
Subject(s) - sh3 domain , polyproline helix , computational biology , peptide , binding selectivity , sh2 domain , molecular recognition , domain (mathematical analysis) , biology , sequence (biology) , chemistry , biochemistry , phosphorylation , proto oncogene tyrosine protein kinase src , mathematics , molecule , mathematical analysis , organic chemistry
Protein interaction domain families that modulate the formation of macromolecular complexes recognize specific sequence or structural motifs. For instance SH3 and WW domains bind to polyproline peptides while SH2 and FHA domains bind to peptides phosphorylated in Tyr and Thr respectively. Within each family, variations in the chemical characteristics of the domain binding pocket modulate a finer peptide recognition specificity and, as a consequence, determine the selection of functional protein partners in vivo. In the proteomic era there is the need for reliable inference methods to help restricting the sequence space of the putative targets to be confirmed experimentally by more laborious experimental approaches. Here we will review the published data about the peptide recognition specificity of the SH3 domain family and we will propose a classification of SH3 domains into eight classes. Finally, we will discuss whether the available information is sufficient to infer the recognition specificity of any uncharacterized SH3 domain.