Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

Article Abstract:

The SH2 domain of the v-src tyrosine kinase, one of the 100 amino acid residues that help the protein-tyrosine kinases accomplish the phosphorylation essential for cellular signal transduction, consists of a middle antiparallel beta-sheet with two alpha-helices with peptides arranged on either side. The structure of the SH2 domain with the v-src oncogene product and two phosphotyrosyl peptides was verified using X-ray crystallography. For cells to recognize phosphotyrosine, amino-aromatic interactions must take place between lysine and arginine side chains and the ring system along with the hydrogen-bonding of phosphate.

Peptides, Cellular signal transduction

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Crystal structure of the Src family tyrosine kinase Hck

Article Abstract:

The crystal structure of the Src family tyrosine kinase haematopoietic cell kinase (Hck) has been determined at 2.6/2.9 A resolution. The SH2 domain is linked to the C-terminal phosphorylated tail but is away from the active site. The linker connecting the SH2 domain to the catalytic domain creates a polyproline type II helix, which functions as the docking site for the SH3 domain. It seems that the SH2 domain serves to position the SH3 binding site.

Molecular structure

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Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement

Article Abstract:

SH2 and SH3 domains have different roles in modulating the activity of Hck. There is a large increase in Hck catalytic activity when the HIV-1 Nef protein is added to either the downregulated or activated form of Hck. The intact SH3-binding motif in Nef is very important for Hck activation. There are findings to indicate that binding of the Hck SH3 domain by Nef leads to an increased activation of the enzyme than does SH2 domain binding.

Enzymes, Phosphorylation, Enzyme regulation

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