5hck
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(New page: 200px<br /> <applet load="5hck" size="450" color="white" frame="true" align="right" spinBox="true" caption="5hck" /> '''HUMAN HCK SH3 DOMAIN, NMR, MINIMIZED AVERAG...)
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Revision as of 21:45, 12 November 2007
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HUMAN HCK SH3 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
SH3 domains are protein binding domains that occur widely among signal, transduction proteins. Here, we present the NMR-determined solution, structure of the SH3 domain from the cytoplasmic protein tyrosine kinase, Hck. Hck is involved in a number of cell signal transduction pathways, frequently in pathways associated with immune response. SH3 domains bind, proteins via a left-handed polyproline type II helix on the target, protein. We have assessed the structural impact of binding to a ligand, through addition of a peptide corresponding to a proline-rich region of a, Hck target, the GTPase activating protein of the Ras pathway. Ligand, binding effects small structural changes and stabilizes the SH3 domain, structure. Also, we have compared the solution structure of the Hck SH3, domain to the crystal structure of Hck, in which the SH3 domain exhibits, an intramolecular binding to an interdomain linker region. These, structures are interpreted as the apo- and holo- forms of the Hck SH3, domain.
About this Structure
5HCK is a Single protein structure of sequence from Homo sapiens. Active as Transferase, with EC number 2.1.7.112 Full crystallographic information is available from OCA.
Reference
Solution structure of the human Hck SH3 domain and identification of its ligand binding site., Horita DA, Baldisseri DM, Zhang W, Altieri AS, Smithgall TE, Gmeiner WH, Byrd RA, J Mol Biol. 1998 Apr 24;278(1):253-65. PMID:9571048
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