Article Abstract:
Shc is an SH2 domain protein involved in signal transduction that is tyrosine phosphorylated after cell induction by different cytokines and growth factors. Amino acids 46-209 of the 52 kDa form of Shc constitute the minimum binding region of Shc amino terminus that facilitates phosphotyrosine-dependent interactions. This phosphotyrosine interaction domain (PID) is nearly 160 amino acids long and has an antiparallel beta sheet, as suggested by the arrangement of beta strands and helices. The PID of Shc is essential for tyrosine kinase signal transduction.
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Article Abstract:
The 3-dimensional structure of the Src homology 3 domain (SH3) in the p85 subunit of the phosphatidylinositol 3-kinase (PI3K) was characterized using multidimensional nuclear magnetic resonance methods. The aim was to gain more understanding of the function of Src homology 3 (SH3) domains in mediating specific protein-protein interactions. The results showed that the ligand-binding properties of the binding sites in the PI3K and the Src SH3 domains may differ even though the overall structures of the binding sites are similar.
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Article Abstract:
TOR and FRAP are novel protein kinases whose kinase domains are necessary for the functioning of TOR2, the G1 cell cycle and other cellular processes. The kinase activity of TOR is not inhibited by FKBP 12-rapamycin but the phosphorylation of G1 effectors is hindered.
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