Rapid Identification of Phosphopeptide Ligands for SH2 Domains
نویسندگان
چکیده
منابع مشابه
Visualizing the Induced Binding of SH2-Phosphopeptide.
Approximately 100 proteins in the human genome contain an SH2 domain recognizing small flexible phosphopeptides. It is therefore important to understand in atomistic detail the way these peptides bind and the conformational changes that take place upon binding. Here, we obtained several spontaneous binding events between the p56 lck SH2 domain and the pYEEI peptide within 2 Å RMSD from the crys...
متن کاملProbing the phosphopeptide specificities of protein tyrosine phosphatases, SH2 and PTB domains with combinatorial library methods.
Protein tyrosine phosphatases, SH2 and PTB domains are crucial elements for cellular signal transduction and regulation. Much effort has been directed towards elucidating their specificity in the past decade using a variety of approaches. Combinatorial library methods have contributed significantly to the understanding of substrate and ligand specificity of phosphoprotein recognizing domains. T...
متن کاملZIP codes for delivering SH2 domains
Around the year 1990, it was discovered that src-homol-ogy 2 (SH2) domains could bind to phosphotyrosine A number of proteins implicated in protein-tyrosine kinase signaling pathways were known to contain SH2 domains, and this discovery revealed how these proteins could form multimeric signaling complexes in response to activation of growth factor receptor family protein-Tyr kinases. However, t...
متن کاملCalorimetric examination of high-affinity Src SH2 domain-tyrosyl phosphopeptide binding: dissection of the phosphopeptide sequence specificity and coupling energetics.
SH2 domains are protein modules which interact with specific tyrosine phosphorylated sequences in target proteins. The SH2 domain of the Src kinase binds with high affinity to a tyrosine phosphorylated peptide containing the amino acids Glu, Glu, and Ile (EEI) at the positions +1, +2, and +3 C-terminal to the phosphotyrosine, respectively. To investigate the degree of selectivity of the Src SH2...
متن کاملAtomistic Modelling of Phosphopeptide Recognition for Modular Domains
This review aims at discussing the molecular details of binding specificity, promiscuity and mechanisms of phosphopeptide recognition to modular domains using computational tools. Protein–phosphoprotein interactions are the driving forces that underline multiple signalling events which are important in cellular function. Understanding protein–phosphopeptide recognition assists designing phospho...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.28.16500