2iej

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{{Seed}}
 
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[[Image:2iej.png|left|200px]]
 
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==Human Protein Farnesyltransferase Complexed with Inhibitor Compound STN-48 And FPP Analog at 1.8A Resolution==
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The line below this paragraph, containing "STRUCTURE_2iej", creates the "Structure Box" on the page.
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<StructureSection load='2iej' size='340' side='right'caption='[[2iej]], [[Resolution|resolution]] 1.80&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'>[[2iej]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IEJ 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]] 1.8&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FII:[(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-METHYL]-PHOSPHONIC+ACID'>FII</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</scene>, <scene name='pdbligand=S48:METHYL+N-{(3S)-1-[(1-METHYL-1H-IMIDAZOL-5-YL)METHYL]-6-PHENYL-1,2,3,4-TETRAHYDROQUINOLIN-3-YL}-N-[(1-METHYL-1H-IMIDAZOL-4-YL)SULFONYL]GLYCINATE'>S48</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2iej| PDB=2iej | 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=2iej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iej OCA], [https://pdbe.org/2iej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iej RCSB], [https://www.ebi.ac.uk/pdbsum/2iej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iej ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FNTA_HUMAN FNTA_HUMAN] 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/ie/2iej_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=2iej ConSurf].
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<div style="clear:both"></div>
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===Human Protein Farnesyltransferase Complexed with Inhibitor Compound STN-48 And FPP Analog at 1.8A 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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</StructureSection>
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The line below this paragraph, {{ABSTRACT_PUBMED_17208314}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 17208314 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17208314}}
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==About this Structure==
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2IEJ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IEJ OCA].
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==Reference==
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Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase., Eastman RT, White J, Hucke O, Yokoyama K, Verlinde CL, Hast MA, Beese LS, Gelb MH, Rathod PK, Van Voorhis WC, Mol Biochem Parasitol. 2007 Mar;152(1):66-71. Epub 2006 Dec 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17208314 17208314]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Protein farnesyltransferase]]
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[[Category: Beese LS]]
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[[Category: Beese, L S.]]
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[[Category: Hast MA]]
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[[Category: Hast, M A.]]
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[[Category: Caax]]
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[[Category: Cancer]]
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[[Category: Falciparum]]
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[[Category: Farnesyl transferase]]
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[[Category: Farnesyltransferase]]
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[[Category: Ftase]]
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[[Category: Lipid modification]]
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[[Category: Malaria]]
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[[Category: Plasmodium]]
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[[Category: Protein prenylation]]
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[[Category: Ra]]
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[[Category: Stn-48]]
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[[Category: Tumor regression]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:27:21 2008''
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Current revision

Human Protein Farnesyltransferase Complexed with Inhibitor Compound STN-48 And FPP Analog at 1.8A Resolution

PDB ID 2iej

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