1ft1
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(New page: 200px<br /><applet load="1ft1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ft1, resolution 2.25Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 13:07, 20 November 2007
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CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION
Overview
Protein farnesyltransferase (FTase) catalyzes the carboxyl-terminal, lipidation of Ras and several other cellular signal transduction proteins., The essential nature of this modification for proper function of these, proteins has led to the emergence of FTase as a target for the development, of new anticancer therapy. Inhibition of this enzyme suppresses the, transformed phenotype in cultured cells and causes tumor regression in, animal models. The crystal structure of heterodimeric mammalian FTase was, determined at 2.25 angstrom resolution. The structure shows a combination, of two unusual domains: a crescent-shaped seven-helical hairpin domain and, an alpha-alpha barrel domain. The active site is formed by two clefts that, intersect at a bound zinc ion. One cleft contains a nine-residue peptide, that may mimic the binding of the Ras substrate; the other cleft is lined, with highly conserved aromatic residues appropriate for binding the, farnesyl isoprenoid with required specificity.
About this Structure
1FT1 is a Protein complex structure of sequences from Rattus norvegicus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution., Park HW, Boduluri SR, Moomaw JF, Casey PJ, Beese LS, Science. 1997 Mar 21;275(5307):1800-4. PMID:9065406
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