PTB or not PTB – that is the question

FEBS Letters

Kuti, Miklos¹  Yan, Kelley S¹  Zhou, Ming-Ming¹ 

[1] Structural Biology Program, Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York University, 1425 Madison Avenue, P.O. Box 1677, New York, NY 10029-6574, USA

关键词: Phosphotyrosine binding domain;    Three-dimensional structure;    Fibroblast growth factor receptor substrate 2;    Insulin receptor substrate-1;    Numb;    Shc;    Suc1-associated neurotrophic factor target;    X11;    β-APP;    β-amyloid precursor protein;    FGFR1;    fibroblast growth factor receptor 1;    IR;    insulin receptor;    IRS;    insulin receptor substrate;    IL-4R;    interleukin-4 receptor;    PH;    pleckstrin homology;    PTB;    phosphotyrosine binding;    SH2;    src homology 2;    SNT;    suc1-associated neurotrophic factor target;    TRK;    tyrosine receptor kinase;   

DOI  :  10.1016/S0014-5793(01)03305-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown