The identification of conserved interactions within the SH3 domain by alignment of sequences and structures.
about
A novel Src homology 2 domain-containing molecule, Src-like adapter protein-2 (SLAP-2), which negatively regulates T cell receptor signalingIdentification and functional analysis of a new phosphorylation site (Y398) in the SH3 domain of Abi-1The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53Atypical polyproline recognition by the CMS N-terminal Src homology 3 domainStructural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinityA unique set of SH3-SH3 interactions controls IB1 homodimerization.Structure of melanoma inhibitory activity protein, a member of a recently identified family of secreted proteinsHepatitis C virus NS5A protein binds the SH3 domain of the Fyn tyrosine kinase with high affinity: mutagenic analysis of residues within the SH3 domain that contribute to the interactionGW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands.Determinants of the Src Homology Domain 3-Like FoldStructural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domainDistinct Peptide Binding Specificities of Src Homology 3 (SH3) Protein Domains Can Be Determined by Modulation of Local Energetics across the Binding InterfaceThe biologically relevant targets and binding affinity requirements for the function of the yeast actin-binding protein 1 Src-homology 3 domain vary with genetic contextInteraction with the SH3 domain protein Bem1 regulates signaling by the Saccharomyces cerevisiae p21-activated kinase Ste20Yeast adaptor protein, Nbp2p, is conserved regulator of fungal Ptc1p phosphatases and is involved in multiple signaling pathwaysConformational coupling between receptor and kinase binding sites through a conserved salt bridge in a signaling complex scaffold proteinFrom Binding-Induced Dynamic Effects in SH3 Structures to Evolutionary Conserved SectorsElectrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formationAdaptor proteins intersectin 1 and 2 bind similar proline-rich ligands but are differentially recognized by SH2 domain-containing proteinsIdentification of a region in p47phox/NCF1 crucial for phagocytic NADPH oxidase (NOX2) activation.The impact of either 4-R-hydroxyproline or 4-R-fluoroproline on the conformation and SH3m-cort binding of HPK1 proline-rich peptide.Functional mechanisms and roles of adaptor proteins in abl-regulated cytoskeletal actin dynamics.Localization of SH3PXD2B in human eyes and detection of rare variants in patients with anterior segment diseases and glaucomaA residue in helical conformation in the native state adopts a β-strand conformation in the folding transition state despite its high and canonical Φ-value.SH3 domain-mediated recruitment of host cell amphiphysins by alphavirus nsP3 promotes viral RNA replicationSolution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP.A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function.Comparison of the frequency of functional SH3 domains with different limited sets of amino acids using mRNA display.The SH3 domain of HS1 protein recognizes lysine-rich polyproline motifs.The ß subunit of voltage-gated Ca2+ channelsAutoinhibition of GEF activity in Intersectin 1 is mediated by the short SH3-DH domain linker.o-Nitrotyrosine and p-iodophenylalanine as spectroscopic probes for structural characterization of SH3 complexes.Structural basis of Robo proline-rich motif recognition by the srGAP1 Src homology 3 domain in the Slit-Robo signaling pathway.Regulation of RhoGEF activity by intramolecular and intermolecular SH3 domain interactions.Transactivation of Abl by the Crk II adapter protein requires a PNAY sequence in the Crk C-terminal SH3 domain.Hydrogen exchange and ligand binding: ligand-dependent and ligand-independent protection in the Src SH3 domain.Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.Transition states for protein folding have native topologies despite high structural variability.The response of internal dynamics to hydrophobic core mutations in the SH3 domain from the Fyn tyrosine kinaseItk phosphorylation sites are required for functional activity in primary T cells.
P2860
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P2860
The identification of conserved interactions within the SH3 domain by alignment of sequences and structures.
description
2000 nî lūn-bûn
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2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
@wuu
name
The identification of conserve ...... t of sequences and structures.
@ast
The identification of conserve ...... t of sequences and structures.
@en
type
label
The identification of conserve ...... t of sequences and structures.
@ast
The identification of conserve ...... t of sequences and structures.
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prefLabel
The identification of conserve ...... t of sequences and structures.
@ast
The identification of conserve ...... t of sequences and structures.
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P2860
P356
P1433
P1476
The identification of conserve ...... t of sequences and structures.
@en
P2093
Davidson AR
P2860
P304
P356
10.1110/PS.9.11.2170
P577
2000-11-01T00:00:00Z