Premium
PTB or not PTB – that is the question
Author(s) -
Yan Kelley S,
Kuti Miklos,
Zhou Ming-Ming
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)03305-1
Subject(s) - computational biology , phosphotyrosine binding domain , biology , context (archaeology) , homology (biology) , function (biology) , protein structure , functional diversity , conserved sequence , microbiology and biotechnology , genetics , sh2 domain , signal transduction , proto oncogene tyrosine protein kinase src , peptide sequence , biochemistry , gene , ecology , paleontology
Phosphotyrosine binding (PTB) domains are structurally conserved modules found in proteins involved in numerous biological processes including signaling through cell‐surface receptors and protein trafficking. While their original discovery is attributed to the recognition of phosphotyrosine in the context of NPXpY sequences – a function distinct from that of the classical src homology 2 (SH2) domain – recent studies show that these protein modules have much broader ligand binding specificities. These studies highlight the functional diversity of the PTB domain family as generalized protein interaction domains, and reinforce the concept that evolutionary changes of structural elements around the ligand binding site on a conserved structural core may endow these protein modules with the structural plasticity necessary for functional versatility.