Structural basis for specificity of GRB2-SH2 revealed by a novel ligand binding mode-Reference-Cited by-同舟云学术

Structural basis for specificity of GRB2-SH2 revealed by a novel ligand binding mode

Published:1996-07 Issue:7 Volume:3 Page:586-589
ISSN:1072-8368
Container-title:Nature Structural Biology
language:
Short-container-title:Nat Struct Mol Biol

Author:

Rahuel Joseph,Gay Brigitte,Erdmann Dirk,Strauss André,García-Echeverría Carlos,Furet Pascal,Caravatti Giorgio,Fretz Heinz,Schoepfer Joseph,Grütter Markus G.

Publisher

Springer Science and Business Media LLC

Subject

Genetics,Biochemistry,Structural Biology

Reference38 articles.

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

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

3. Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor

4. Human Sos1: a Guanine Nucleotide Exchange Factor for Ras that Binds to GRB2

5. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation

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