Title : Molecular dynamics simulations reveal that Tyr-317 phosphorylation reduces Shc binding affinity for phosphotyrosyl residues of epidermal growth factor receptor.

Pub. Date : 2009 Mar 18

PMID : 19289054






8 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Molecular dynamics simulations reveal that Tyr-317 phosphorylation reduces Shc binding affinity for phosphotyrosyl residues of epidermal growth factor receptor. Tyrosine SHC adaptor protein 1 Homo sapiens
2 Shc binding to phospho-tyrosine residues on activated receptors is mediated by the SH2 and phospho-tyrosine binding (PTB) domains. Tyrosine SHC adaptor protein 1 Homo sapiens
3 Shc binding to phospho-tyrosine residues on activated receptors is mediated by the SH2 and phospho-tyrosine binding (PTB) domains. Tyrosine SHC adaptor protein 1 Homo sapiens
4 Subsequent phosphorylation on Tyr-317 within the Shc linker region induces Shc interactions with Grb2-Son of Sevenless that initiate Ras-mitogen-activated protein kinase signaling. Tyrosine SHC adaptor protein 1 Homo sapiens
5 Subsequent phosphorylation on Tyr-317 within the Shc linker region induces Shc interactions with Grb2-Son of Sevenless that initiate Ras-mitogen-activated protein kinase signaling. Tyrosine SHC adaptor protein 1 Homo sapiens
6 Our simulations reveal that Shc tyrosine phosphorylation results in a significant rearrangement of the relative position of its domains, suggesting a key conformational change. Tyrosine SHC adaptor protein 1 Homo sapiens
7 Our results unveil what we believe is a novel structural phenomenon, i.e., tyrosine phosphorylation of Shc within its linker region regulates the binding affinity of SH2 and PTB domains for phosphorylated Shc partners, with important implications for signaling dynamics. Tyrosine SHC adaptor protein 1 Homo sapiens
8 Our results unveil what we believe is a novel structural phenomenon, i.e., tyrosine phosphorylation of Shc within its linker region regulates the binding affinity of SH2 and PTB domains for phosphorylated Shc partners, with important implications for signaling dynamics. Tyrosine SHC adaptor protein 1 Homo sapiens