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1ft1

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[[Image:1ft1.gif|left|200px]]
 
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==CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION==
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The line below this paragraph, containing "STRUCTURE_1ft1", creates the "Structure Box" on the page.
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<StructureSection load='1ft1' size='340' side='right'caption='[[1ft1]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ft1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FT1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1ft1| PDB=1ft1 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ft1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ft1 OCA], [https://pdbe.org/1ft1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ft1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ft1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ft1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FNTA_RAT FNTA_RAT] Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ft/1ft1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ft1 ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION'''
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==See Also==
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*[[Farnesyltransferase 3D structures|Farnesyltransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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1FT1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FT1 OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9065406 9065406]
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[[Category: Protein complex]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Beese, L S.]]
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[[Category: Beese LS]]
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[[Category: Park, H W.]]
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[[Category: Park H-W]]
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[[Category: Cancer therapeutic]]
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[[Category: G protein]]
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[[Category: Prenyltransferase]]
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[[Category: Ra]]
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[[Category: Signal transduction]]
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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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Current revision

CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION

PDB ID 1ft1

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