Mona/Gads SH3C binding to hematopoietic progenitor kinase 1 (HPK1) combines an atypical SH3 binding motif, R/KXXK, with a classical PXXP motif embedded in a polyproline type II (PPII) helix
about
Efficient T-cell receptor signaling requires a high-affinity interaction between the Gads C-SH3 domain and the SLP-76 RxxK motifRegulation and function of SKAP-55 non-canonical motif binding to the SH3c domain of adhesion and degranulation-promoting adaptor proteinNovel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich regionExpression, refolding and crystallizations of the Grb2-like (GADS) C-terminal SH3 domain complexed with a SLP-76 motif peptideStructural basis for recognition of the third SH3 domain of full-length R85 (R85FL)/ponsin by ataxin-7Regulation of epidermal growth factor receptor ubiquitination and trafficking by the USP8·STAM complexGrb2-SH3 ligand inhibits the growth of HER2+ cancer cells and has antitumor effects in human cancer xenografts alone and in combination with docetaxelSH3 domain ligand binding: What's the consensus and where's the specificity?Structural, Functional, and Bioinformatic Studies Demonstrate the Crucial Role of an Extended Peptide Binding Site for the SH3 Domain of Yeast Abp1pEnterohaemorrhagic Escherichia Coli Exploits a Tryptophan Switch to Hijack Host F-Actin AssemblyDistinct Peptide Binding Specificities of Src Homology 3 (SH3) Protein Domains Can Be Determined by Modulation of Local Energetics across the Binding InterfaceInhibition of D-serine accumulation in the Xenopus oocyte by expression of the rat ortholog of human 3'-phosphoadenosine 5'-phosphosulfate transporter gene isolated from the neocortex as D-serine modulator-1Evolution of domain-peptide interactions to coadapt specificity and affinity to functional diversityGrb2 carboxyl-terminal SH3 domain can bivalently associate with two ligands, in an SH3 dependent manner.Exhaustive search of linear information encoding protein-peptide recognitionQuantitative analysis by surface plasmon resonance of CD28 interaction with cytoplasmic adaptor molecules Grb2, Gads and p85 PI3K.Coordinated activation of the Rac-GAP β2-chimaerin by an atypical proline-rich domain and diacylglycerol.GRB2-mediated recruitment of THEMIS to LAT is essential for thymocyte development.Novel inhibitors of a Grb2 SH3C domain interaction identified by a virtual screenInterfacial water molecules in SH3 interactions: Getting the full picture on polyproline recognition by protein-protein interaction domains.Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transductionA Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function.The SH3 domain of HS1 protein recognizes lysine-rich polyproline motifs.Intracellular protein interaction mapping with FRET hybrids.Structural basis for recognition of the T cell adaptor protein SLP-76 by the SH3 domain of phospholipase Cgamma1A new family of intrinsically disordered proteins: structural characterization of the major phasin PhaF from Pseudomonas putida KT2440Protein phosphatase 4 is a positive regulator of hematopoietic progenitor kinase 1.Secondary structure, a missing component of sequence-based minimotif definitions.Crystallization and preliminary X-ray analysis of the GST-fused human Bri3 N-terminal domainActivation of hematopoietic progenitor kinase 1 involves relocation, autophosphorylation, and transphosphorylation by protein kinase D1.Structural features of the full-length adaptor protein GADS in solution determined using small-angle X-ray scattering.
P2860
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P2860
Mona/Gads SH3C binding to hematopoietic progenitor kinase 1 (HPK1) combines an atypical SH3 binding motif, R/KXXK, with a classical PXXP motif embedded in a polyproline type II (PPII) helix
description
2004 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2004
@ast
im Juli 2004 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2004/07/02)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/07/02)
@nl
наукова стаття, опублікована в липні 2004
@uk
name
Mona/Gads SH3C binding to hema ...... lyproline type II (PPII) helix
@ast
Mona/Gads SH3C binding to hema ...... lyproline type II (PPII) helix
@en
Mona/Gads SH3C binding to hema ...... lyproline type II (PPII) helix
@nl
type
label
Mona/Gads SH3C binding to hema ...... lyproline type II (PPII) helix
@ast
Mona/Gads SH3C binding to hema ...... lyproline type II (PPII) helix
@en
Mona/Gads SH3C binding to hema ...... lyproline type II (PPII) helix
@nl
prefLabel
Mona/Gads SH3C binding to hema ...... lyproline type II (PPII) helix
@ast
Mona/Gads SH3C binding to hema ...... lyproline type II (PPII) helix
@en
Mona/Gads SH3C binding to hema ...... lyproline type II (PPII) helix
@nl
P2093
P2860
P921
P356
P1476
Mona/Gads SH3C binding to hema ...... lyproline type II (PPII) helix
@en
P2093
Marc Lewitzky
Maria Harkiolaki
Stephan M. Feller
P2860
P304
28724–28732
P356
10.1074/JBC.M402745200
P407
P577
2004-07-02T00:00:00Z