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2bed

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Revision as of 07:27, 18 October 2017

Structure of FPT bound to inhibitor SCH207736

Structural highlights

2bed 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)
Activity:	Protein farnesyltransferase, with EC number 2.5.1.58
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

Benzocycloheptapyridine tricyclic compounds with piperazine or substituted piperidine moieties extending either from the 5- or 6-position of the tricyclic bridgehead exhibited enhanced FTase activity: this resulted from favorable binding of the ligand nitrogen with the catalytic zinc found in the FTase. A single isomer at C-11 with piperazine adduct extending from the 6-position, compound 24, exhibited excellent FTase activity with IC50 = 0.007 microM, soft agar IC50 = 72 nM, and Rat AUC(PO, 10 mpk) = 4.0 microM x h. X-ray of (-)-[8-chloro-6-(1-piperazinyl)-1H-benzo[5,6]]cyclohepta[1,2-b]pyridine-11 -yl]-1-(methylsulfonyl)piperidine 24 bound to Ftase revealed favorable interaction between piperazine nitrogen and catalytic zinc atom.

Enhanced FTase activity achieved via piperazine interaction with catalytic zinc.,Njoroge FG, Vibulbhan B, Pinto P, Strickland C, Bishop WR, Nomeir A, Girijavallabhan V Bioorg Med Chem Lett. 2006 Feb 15;16(4):984-8. Epub 2005 Nov 16. PMID:16298128^[1]

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

References

↑ Njoroge FG, Vibulbhan B, Pinto P, Strickland C, Bishop WR, Nomeir A, Girijavallabhan V. Enhanced FTase activity achieved via piperazine interaction with catalytic zinc. Bioorg Med Chem Lett. 2006 Feb 15;16(4):984-8. Epub 2005 Nov 16. PMID:16298128 doi:10.1016/j.bmcl.2005.10.090

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/2bed"

@@ Line 1: / Line 1: @@
 ==Structure of FPT bound to inhibitor SCH207736==
 <StructureSection load='2bed' size='340' side='right' caption='[[2bed]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_farnesyltransferase Protein farnesyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.58 2.5.1.58] </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=2bed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bed OCA], [http://pdbe.org/2bed PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bed RCSB], [http://www.ebi.ac.uk/pdbsum/2bed 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=2bed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bed OCA], [http://pdbe.org/2bed PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bed RCSB], [http://www.ebi.ac.uk/pdbsum/2bed PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bed ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 2bed" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Farnesyltransferase|Farnesyltransferase]]
 == References ==
 <references/>

2bed

From Proteopedia

Revision as of 07:27, 18 October 2017

Structure of FPT bound to inhibitor SCH207736

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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