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1nl4

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Revision as of 16:29, 12 October 2017

Crystal Structure of Rat Farnesyl Transferase in Complex With A Potent Biphenyl Inhibitor

Structural highlights

1nl4 is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	FNTA (Buffalo rat), FNTB (Buffalo rat)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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). [FNTB_RAT] Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

A series of imidazole-containing biphenyls was prepared and evaluated in vitro for inhibition of FTase and cellular Ras processing. Several of these analogues, such as 21, are potent inhibitors of FTase (<1nM), FTase/GGTase selective (>300-fold) and cellularly active (<or=80nM). An X-ray crystal structure of inhibitor 21 bound to rat farnesyltransferase is also presented.

Novel and selective imidazole-containing biphenyl inhibitors of protein farnesyltransferase.,Curtin ML, Florjancic AS, Cohen J, Gu WZ, Frost DJ, Muchmore SW, Sham HL Bioorg Med Chem Lett. 2003 Apr 7;13(7):1367-71. PMID:12657284^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Curtin ML, Florjancic AS, Cohen J, Gu WZ, Frost DJ, Muchmore SW, Sham HL. Novel and selective imidazole-containing biphenyl inhibitors of protein farnesyltransferase. Bioorg Med Chem Lett. 2003 Apr 7;13(7):1367-71. PMID:12657284

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nl4"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Rat Farnesyl Transferase in Complex With A Potent Biphenyl Inhibitor==
 <StructureSection load='1nl4' size='340' side='right' caption='[[1nl4]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FTL:4-[(3-CYANO-BENZYL)-(3-METHYL-3H-IMIDAZOL-4-YLMETHYL)-AMINO]-2-NAPHTHALEN-1-YL-BENZONITRILE'>FTL</scene>, <scene name='pdbligand=HFP:ALPHA-HYDROXYFARNESYLPHOSPHONIC+ACID'>HFP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FNTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), FNTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nl4 OCA], [http://pdbe.org/1nl4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nl4 RCSB], [http://www.ebi.ac.uk/pdbsum/1nl4 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nl4 OCA], [http://pdbe.org/1nl4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nl4 RCSB], [http://www.ebi.ac.uk/pdbsum/1nl4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nl4 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata 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=1nl4 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1nl4" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Farnesyltransferase|Farnesyltransferase]]
 == References ==
 <references/>

1nl4

From Proteopedia

Revision as of 16:29, 12 October 2017

Crystal Structure of Rat Farnesyl Transferase in Complex With A Potent Biphenyl Inhibitor

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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