1n94: Difference between revisions
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<StructureSection load='1n94' size='340' side='right'caption='[[1n94]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='1n94' size='340' side='right'caption='[[1n94]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1n94]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1n94]] 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=1N94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N94 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HFP:ALPHA-HYDROXYFARNESYLPHOSPHONIC+ACID'>HFP</scene>, <scene name='pdbligand=TIN:2-{(5-{[BUTYL-(2-CYCLOHEXYL-ETHYL)-AMINO]-METHYL}-2-METHYL-BIPHENYL-2-CARBONYL)-AMINO]-4-METHYLSULFANYL-BUTYRIC+ACID'>TIN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HFP:ALPHA-HYDROXYFARNESYLPHOSPHONIC+ACID'>HFP</scene>, <scene name='pdbligand=TIN:2-{(5-{[BUTYL-(2-CYCLOHEXYL-ETHYL)-AMINO]-METHYL}-2-METHYL-BIPHENYL-2-CARBONYL)-AMINO]-4-METHYLSULFANYL-BUTYRIC+ACID'>TIN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n94 OCA], [https://pdbe.org/1n94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n94 RCSB], [https://www.ebi.ac.uk/pdbsum/1n94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n94 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n94 OCA], [https://pdbe.org/1n94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n94 RCSB], [https://www.ebi.ac.uk/pdbsum/1n94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n94 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1n94 ConSurf]. | </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=1n94 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Farnesyltransferase 3D structures|Farnesyltransferase 3D structures]] | *[[Farnesyltransferase 3D structures|Farnesyltransferase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Cohen J]] | ||
[[Category: Gu | [[Category: Gu WZ]] | ||
[[Category: | [[Category: Gwaltney II SL]] | ||
[[Category: | [[Category: Hasvold L]] | ||
[[Category: Imade | [[Category: Imade H]] | ||
[[Category: Li | [[Category: Li Q]] | ||
[[Category: Nelson | [[Category: Nelson LT]] | ||
[[Category: | [[Category: O'Connor SJ]] | ||
[[Category: | [[Category: Sullivan GM]] | ||
[[Category: | [[Category: Wang W]] | ||
Revision as of 11:47, 10 April 2024
Aryl Tetrahydropyridine Inhbitors of Farnesyltransferase: Glycine, Phenylalanine and Histidine DerivatesAryl Tetrahydropyridine Inhbitors of Farnesyltransferase: Glycine, Phenylalanine and Histidine Derivates
Structural highlights
FunctionFNTA_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). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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