Member database | PRINTS |
PRINTS type | domain |
Short name | SHCPIDOMAIN |
Description Imported from IPR006019
Shc proteins contain an SH2 domain and a phosphotyrosine interaction (PI) domain. These domains facilitate interaction with various activated tyrosine-phosphorylated receptors, including those of growth factors, insulin, cytokines and lymphocytes. The PI domain comprises 165 residues, 4 of which (Arg67, Arg175, Ser151 and Lys169
[1]) are responsible for binding phosphotyrosine on a `IIENPQYFSDA'(NPxPY) peptide
[2].
The PI domain has a similar structure to the insulin receptor substrate-1 PTB domain, a 7-stranded β-sandwich, capped by a C-terminal helix. However, the PI domain contains an additional short N-terminal helix and a large insertion between strands 1 and 2, which forms a helix and 2 long connecting loops. The substrate peptide fits into a surface cleft formed from the C-terminal helix and strand 5
[3].
References Imported from IPR006019
1.Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor. Eck MJ, Dhe-Paganon S, Trub T, Nolte RT, Shoelson SE. Cell 85, 695-705, (1996). View articlePMID: 8646778
2.Shc binding to nerve growth factor receptor is mediated by the phosphotyrosine interaction domain. Dikic I, Batzer AG, Blaikie P, Obermeier A, Ullrich A, Schlessinger J, Margolis B. J. Biol. Chem. 270, 15125-9, (1995). View articlePMID: 7541035
3.Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain. Zhou MM, Huang B, Olejniczak ET, Meadows RP, Shuker SB, Miyazaki M, Trub T, Shoelson SE, Fesik SW. Nat. Struct. Biol. 3, 388-93, (1996). View articlePMID: 8599766
Supplementary References
Integrated to
Representative structure
4xwx: Crystal structure of the PTB domain of SHC