1QG1

GROWTH FACTOR RECEPTOR BINDING PROTEIN SH2 DOMAIN COMPLEXED WITH AN SHC-DERIVED PEPTIDE

Summary for 1QG1

• Entry DOI: 10.2210/pdb1qg1/pdb
• Descriptor: PROTEIN (GROWTH FACTOR RECEPTOR BINDING PROTEIN), PROTEIN (SHC-DERIVED PEPTIDE) (2 entities in total)
• Functional Keywords: signal transduction, sh2 domain, phosphotyrosyl peptide, complex (signal transduction-peptide), hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human); More
• Cellular location: Golgi apparatus (By similarity): P62993; Cytoplasm. Isoform p46Shc: Mitochondrion matrix. Isoform p66Shc: Mitochondrion (By similarity): P29353
• Total number of polymer chains: 2
• Total formula weight: 13600.07

Authors

Ogura, K. (deposition date: 1999-04-19, release date: 1999-04-27, Last modification date: 2023-12-27)

Primary citation

Ogura, K.,Tsuchiya, S.,Terasawa, H.,Yuzawa, S.,Hatanaka, H.,Mandiyan, V.,Schlessinger, J.,Inagaki, F.
Solution structure of the SH2 domain of Grb2 complexed with the Shc-derived phosphotyrosine-containing peptide.
J.Mol.Biol., 289:439-445, 1999

PubMed Abstract: The solution structure of growth factor receptor-bound protein 2 (Grb2) SH2 complexed with a Shc-derived phosphotyrosine (pTyr)-containing peptide was determined by nuclear magnetic resonance (NMR) spectroscopy. The pTyr binding site of Grb2 SH2 was similar to those of other SH2 domains. In contrast, the amino acid residues C-terminal to pTyr did not form an extended structure because of steric hindrance caused by a bulky side-chain of Trp121 (EF1). As a result, the peptide formed a turn-structure on the surface of Grb2 SH2. The asparagine residue at the pTyr+2 position of the Shc-peptide interacted with the main-chain carbonyl groups of Lys109 and Leu120. The present solution structure was similar to the crystal structure reported for Grb2 SH2 complexed with a BCR-Abl-derived phosphotyrosine-containing peptide. Finally, the structure of Grb2 SH2 domain was compared with those of the complexes of Src and phospholipase C-gamma1 with their cognate peptides, showing that the specific conformation of the peptide was required for binding to the SH2 domains.

PubMed: 10356320
DOI: 10.1006/jmbi.1999.2792

Experimental method

SOLUTION NMR