Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins (Q28281847)

2

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R Tanimura

3

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H Nakamura

4

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K Matuoka

5

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T Takenawa

6

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K Nagashima

7

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T Kurata

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

14 June 1996

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published in

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volume

271

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issue

24

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page(s)

14468-72

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cites work

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Binding of Transforming Protein, P47 gag-crk , to a Broad Range of Phosphotyrosine-containing Proteins

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Two species of human CRK cDNA encode proteins with distinct biological activities

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The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling

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Cloning of ASH, a ubiquitous protein composed of one Src homology region (SH) 2 and two SH3 domains, from human and rat cDNA libraries

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Both the SH2 and SH3 domains of human CRK protein are required for neuronal differentiation of PC12 cells

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Expression of the v-crk oncogene product in PC12 cells results in rapid differentiation by both nerve growth factor- and epidermal growth factor-dependent pathways

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v-Crk modulation of growth factor-induced PC12 cell differentiation involves the Src homology 2 domain of v-Crk and sustained activation of the Ras/mitogen-activated protein kinase pathway

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CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells

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Signalling through SH2 and SH3 domains

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Protein modules and signalling networks

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The product of the cbl oncogene forms stable complexes in vivo with endogenous Crk in a tyrosine phosphorylation-dependent manner

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DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane

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Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G

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

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

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Structure and function of the SH3 domain

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

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

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SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange

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C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins

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eps15, a novel tyrosine kinase substrate, exhibits transforming activity

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Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk

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The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R

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Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains

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Solution structure and ligand-binding site of the carboxy-terminal SH3 domain of GRB2

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Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites

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Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos.

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Crystal structure of the mammalian Grb2 adaptor

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Backwards and forwards binding

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Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system

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Signalling an interest

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