Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck
about
Tyrosine 319 in the interdomain B of ZAP-70 is a binding site for the Src homology 2 domain of LckStructural characterization of a novel Cbl phosphotyrosine recognition motif in the APS family of adapter proteinsPleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1Tyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphataseStructural determinants of the interaction between the erbB2 receptor and the Src homology 2 domain of Grb7Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptorConstruction of an SH2 domain-binding site with mixed specificityMolecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domainIdentification of amino acid residues critical for the Src-homology 2 domain-dependent docking of Stat2 to the interferon alpha receptorDifferential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1Protein binding and signaling properties of RIN1 suggest a unique effector functionSequence requirements for the recognition of tyrosine-based endocytic signals by clathrin AP-2 complexesRapid identification of phosphopeptide ligands for SH2 domains. Screening of peptide libraries by fluorescence-activated bead sortingSolution structure and backbone dynamics of the non-receptor protein-tyrosine kinase-6 Src homology 2 domainBcr-Abl oncoproteins bind directly to activators of the Ras signalling pathwayStructure of a specific peptide complex of the carboxy-terminal SH2 domain from the p85 alpha subunit of phosphatidylinositol 3-kinaseInteraction of phosphorylated FcepsilonRIgamma immunoglobulin receptor tyrosine activation motif-based peptides with dual and single SH2 domains of p72syk. Assessment of binding parameters and real time binding kineticsPhosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal regionThe human GRB2 and Drosophila Drk genes can functionally replace the Caenorhabditis elegans cell signaling gene sem-5.Kinase activation through dimerization by human SH2-BStructural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cellsVav family proteins couple to diverse cell surface receptorsThe structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5pGenetic analysis of a phosphatidylinositol 3-kinase SH2 domain reveals determinants of specificityThe T-cell antigen CD5 acts as a receptor and substrate for the protein-tyrosine kinase p56lckAutophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60srcSolution structure of the human Grb14-SH2 domain and comparison with the structures of the human Grb7-SH2/erbB2 peptide complex and human Grb10-SH2 domainCrystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor c-Met and its complex with the microbial alkaloid K-252aThe Fyn-ADAP Axis: Cytotoxicity Versus Cytokine Production in Killer CellsStructure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinaseStructure-based design of an osteoclast-selective, nonpeptide src homology 2 inhibitor with in vivo antiresorptive activityStructural basis for dimerization of the Grb10 Src homology 2 domain. Implications for ligand specificityStructural and energetic aspects of Grb2-SH2 domain-swappingGrb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferationA potent and highly specific FN3 monobody inhibitor of the Abl SH2 domainStructure of Lipid Kinase p110β/p85β Elucidates an Unusual SH2-Domain-Mediated Inhibitory MechanismTwo Closely Spaced Tyrosines Regulate NFAT Signaling in B Cells via Syk Association with VavSimultaneous Binding of Two Peptidyl Ligands by a Src Homology 2 DomainWater-refined solution structure of the human Grb7-SH2 domain in complex with the erbB2 receptor peptide pY1139Superbinder SH2 domains act as antagonists of cell signaling
P2860
Q22009540-9987DC10-6D6F-4A9D-B971-17D874AE81CAQ24297076-663DF663-AD64-4BB2-B956-C6219B02EB79Q24304774-133BEA1D-CF5F-4D2F-8989-7C57E26928F4Q24304981-081E3B8E-99C0-445E-904D-A0EDC19B8171Q24310358-2297615C-7033-48B5-BE1E-C48D7CC1F64BQ24311075-140654A1-D286-4D0E-8455-11A6FC41175CQ24315793-6B7566B8-ED87-484C-83AF-E6BCDC602B8FQ24316893-C9E1C7C1-BA60-4D81-83DA-B3D23D73C90CQ24317719-FF9A62A2-443B-4BA4-8876-E1469E26A000Q24319091-C8207D0E-49F1-41D8-B988-F87652706C85Q24319548-CBB4B1F4-ED0B-4CD4-85D1-0B4C1436A4E0Q24319982-9C6F90AA-FACB-4FEF-93E4-CB3683AA4330Q24321244-019DB702-4B4B-4DA5-A390-E42A5976A61CQ24322847-6E00730A-111A-4497-8B7A-48F100DAD2B6Q24324144-F3D64A8D-06E6-4D9F-9BB3-8141102A1249Q24324349-60E31D6A-405E-4E9E-8049-C28C7A2C61BCQ24324474-83A7074C-F419-41CB-A11A-175F6314B175Q24336479-F663A2F0-C15E-4CF0-8E0B-379BD3E8CD41Q24337241-9FDA85A6-BBC9-457A-BEA9-E2F84BECD81CQ24519086-AD35F184-BF88-48C4-9521-C86AD21C4F68Q24535874-3199A219-197B-4FB8-8AC3-1BDAB967A0ECQ24552004-B7C68784-60A4-4A1D-AFD5-F639A3BC1C1AQ24596953-2BD7A8AF-B86E-4342-A955-8A1E39E67F6EQ24610035-3004E80F-FB94-45BA-8AE0-FB62E8F565AAQ24613024-472FBDB7-D425-4672-A7F0-B816441352C2Q24614033-E69D679C-A747-4D53-BA51-BCCA35726135Q24646307-2190DD35-0A08-4375-B538-4102EBA601EEQ24647566-F73E633F-A143-4F78-8243-86B5C7F7C42FQ26781282-ED44EB90-081C-45FB-9790-4FC1417B4741Q27617539-9507831E-4C5D-4E14-A8FC-40D06149F579Q27626519-55F68409-8609-4274-92C2-67C59AD024ECQ27640366-9AE95F76-4D48-4B26-B745-6A10500BABBEQ27644625-E6386784-7CC5-45C6-96FE-B53C4BEB6BDBQ27648499-ECBBEAC9-9789-4ACE-9468-09F485EE8E18Q27660385-A057EECF-8F68-4C19-9971-980B51261350Q27667112-F8390C56-F2AA-4BC3-ADF5-4CE78B7005BBQ27667961-D8D4F1B7-52E5-4238-B083-B6F1FBCCB439Q27671220-430E5FCE-E932-4436-AE00-90F0041E9CC4Q27681182-A055C92F-1FD1-498C-A165-82D1ADB85E3CQ27682496-91CA0C6C-0573-481A-8F4C-82185491AC03
P2860
Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck
description
1993 nî lūn-bûn
@nan
1993 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի մարտին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Recognition of a high-affinity ...... rc homology-2 domain of p56lck
@ast
Recognition of a high-affinity ...... rc homology-2 domain of p56lck
@en
Recognition of a high-affinity ...... rc homology-2 domain of p56lck
@nl
type
label
Recognition of a high-affinity ...... rc homology-2 domain of p56lck
@ast
Recognition of a high-affinity ...... rc homology-2 domain of p56lck
@en
Recognition of a high-affinity ...... rc homology-2 domain of p56lck
@nl
prefLabel
Recognition of a high-affinity ...... rc homology-2 domain of p56lck
@ast
Recognition of a high-affinity ...... rc homology-2 domain of p56lck
@en
Recognition of a high-affinity ...... rc homology-2 domain of p56lck
@nl
P2093
P3181
P356
P1433
P1476
Recognition of a high-affinity ...... rc homology-2 domain of p56lck
@en
P2093
S C Harrison
S E Shoelson
P2888
P3181
P356
10.1038/362087A0
P407
P577
1993-03-04T00:00:00Z
P6179
1001978864