1a81
From Proteopedia
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CRYSTAL STRUCTURE OF THE TANDEM SH2 DOMAIN OF THE SYK KINASE BOUND TO A DUALLY TYROSINE-PHOSPHORYLATED ITAM
Overview
The Syk family of kinases, consisting of ZAP-70 and Syk, play essential, roles in a variety of immune and non-immune cells. This family of kinases, is characterized by the presence of two adjacent SH2 domains which mediate, their localization to the membrane through receptor encoded tyrosine, phosphorylated motifs. While these two kinases share many structural and, functional features, the more ubiquitous nature of Syk has suggested that, this kinase may accommodate a greater variety of motifs to mediate its, function. We present the crystal structure of the tandem SH2 domain of Syk, complexed with a dually phosphorylated ITAM peptide. The structure was, solved by multiple isomorphous replacement at 3.0 A resolution. The, asymmetric unit comprises six copies of the liganded protein, revealing a, surprising flexibility in the relative orientation of the two SH2 domains., The C-terminal phosphotyrosine-binding site is very different from the, equivalent region of ZAP-70, suggesting that in contrast to ZAP-70, the, two SH2 domains of Syk can function as independent units. The, conformational flexibility and structural independence of the SH2 modules, of Syk likely provides the molecular basis for the more ubiquitous, involvement of Syk in a variety of signal transduction pathways.
About this Structure
1A81 is a Protein complex structure of sequences from Homo sapiens. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide., Futterer K, Wong J, Grucza RA, Chan AC, Waksman G, J Mol Biol. 1998 Aug 21;281(3):523-37. PMID:9698567
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