Identification of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains (Q28291074)

1

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C J Soames

2

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L Wilson

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D L Nelson

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D M Stewart

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O Truong

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J J Hsuan

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S Kellie

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

18 October 1996

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published in

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volume

271

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issue

42

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page(s)

26291-5

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cites work

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Src homology region 2 domains direct protein-protein interactions in signal transduction

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SH2 domains recognize specific phosphopeptide sequences

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Association between the PDGF receptor and members of the src family of tyrosine kinases

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GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunit

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Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase

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Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms

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Identification of a ten-amino acid proline-rich SH3 binding site

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Solution structure of the SH3 domain of phospholipase C-gamma

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Motor neurons and neurofilaments in sickness and in health

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Structure of the PI3K SH3 domain and analysis of the SH3 family

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High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides

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Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions

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Structural basis for the binding of proline-rich peptides to SH3 domains

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Phage display selection of ligand residues important for Src homology 3 domain binding specificity

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Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2.

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SH3-dependent assembly of the phagocyte NADPH oxidase

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Isolation of a novel gene mutated in Wiskott-Aldrich syndrome

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Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

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Accelerated high‐sensitivity microsequencing of proteins and peptides using a miniature reaction cartridge

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Studies of the expression of the Wiskott-Aldrich syndrome protein

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Sam68 from an immortalised B-cell line associates with a subset of SH3 domains

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Wiskott-Aldrich syndrome. An immunologic deficiency disease involving the afferent limb of immunity

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Evidence for defective transmembrane signaling in B cells from patients with Wiskott-Aldrich syndrome

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Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization

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The mouse homolog of the Wiskott-Aldrich syndrome protein (WASP) gene is highly conserved and maps near the scurfy (sf) mutation on the X chromosome

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Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains

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Characterization of the interaction of natural proline-rich peptides with five different SH3 domains.

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Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains

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Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain

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A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases

21 January 2018

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Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome

21 January 2018

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Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases

21 January 2018

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Modular binding domains in signal transduction proteins

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Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav

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The Wiskott-Aldrich syndrome. A disorder with a possible defect in antigen processing or recognition.

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