1ft1

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[[Image:1ft1.gif|left|200px]]
[[Image:1ft1.gif|left|200px]]
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{{Structure
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|PDB= 1ft1 |SIZE=350|CAPTION= <scene name='initialview01'>1ft1</scene>, resolution 2.25&Aring;
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The line below this paragraph, containing "STRUCTURE_1ft1", creates the "Structure Box" on the page.
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|SITE=
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|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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{{STRUCTURE_1ft1| PDB=1ft1 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ft1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ft1 OCA], [http://www.ebi.ac.uk/pdbsum/1ft1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ft1 RCSB]</span>
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'''CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION'''
'''CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION'''
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[[Category: Beese, L S.]]
[[Category: Beese, L S.]]
[[Category: Park, H W.]]
[[Category: Park, H W.]]
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[[Category: cancer therapeutic]]
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[[Category: Cancer therapeutic]]
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[[Category: g protein]]
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[[Category: G protein]]
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[[Category: prenyltransferase]]
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[[Category: Prenyltransferase]]
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[[Category: ra]]
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[[Category: Ra]]
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[[Category: signal transduction]]
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[[Category: Signal transduction]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:43:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:29:42 2008''
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Revision as of 13:43, 2 May 2008

Image:1ft1.gif

Template:STRUCTURE 1ft1

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. 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 Page seeded by OCA on Fri May 2 16:43:57 2008

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