FNTB

Farnesyltransferase, CAAX box, beta

PDB rendering based on 1d8d.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1JCQ, 1LD7, 1LD8, 1MZC, 1S63, 1SA4, 1TN6, 2F0Y, 2H6F, 2H6G, 2H6H, 2H6I, 2IEJ, 3E37

Identifiers

Symbols

FNTB ; FPTB

External IDs

OMIM: 134636 MGI: 1861305 HomoloGene: 1535 ChEMBL: 272 GeneCards: FNTB Gene

EC number

2.5.1.58

Gene ontology
Molecular function	• farnesyltranstransferase activity • protein farnesyltransferase activity • protein binding • drug binding • zinc ion binding • isoprenoid binding • peptide binding
Cellular component	• cytosol • microtubule associated complex • protein farnesyltransferase complex
Biological process	• phototransduction, visible light • negative regulation of cell proliferation • response to inorganic substance • response to organic cyclic compound • rhodopsin mediated signaling pathway • protein farnesylation • regulation of rhodopsin mediated signaling pathway • response to cytokine • wound healing • positive regulation of cell cycle • positive regulation of fibroblast proliferation • positive regulation of nitric-oxide synthase biosynthetic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
64.99 – 65.06 Mb

Chr 12:
76.77 – 76.92 Mb

PubMed search

Protein farnesyltransferase subunit beta is an enzyme that in humans is encoded by the FNTB gene.^[1]^[2]

References

↑ Andres DA, Milatovich A, Ozcelik T, Wenzlau JM, Brown MS, Goldstein JL, Francke U (Feb 1994). "cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences". Genomics 18 (1): 105–12. doi:10.1006/geno.1993.1432. PMID 8276393.
↑ "Entrez Gene: FNTB farnesyltransferase, CAAX box, beta".

Manne V, Roberts D, Tobin A; et al. (1990). "Identification and preliminary characterization of protein-cysteine farnesyltransferase.". Proc. Natl. Acad. Sci. U.S.A. 87 (19): 7541–5. doi:10.1073/pnas.87.19.7541. PMC 54783. PMID 2217184.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Sinensky M, Fantle K, Trujillo M; et al. (1994). "The processing pathway of prelamin A". J. Cell. Sci. 107 (1): 61–7. PMID 8175923.
Omer CA, Kral AM, Diehl RE; et al. (1993). "Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases". Biochemistry 32 (19): 5167–76. doi:10.1021/bi00070a028. PMID 8494894.
Wang T, Danielson PD, Li BY; et al. (1996). "The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling". Science 271 (5252): 1120–2. doi:10.1126/science.271.5252.1120. PMID 8599089.
Nantais DE, Schwemmle M, Stickney JT; et al. (1996). "Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1". J. Leukoc. Biol. 60 (3): 423–31. PMID 8830800.
Goalstone ML, Draznin B (1996). "Effect of insulin on farnesyltransferase activity in 3T3-L1 adipocytes". J. Biol. Chem. 271 (44): 27585–9. doi:10.1074/jbc.271.44.27585. PMID 8910345.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Long SB, Casey PJ, Beese LS (1998). "Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate". Biochemistry 37 (27): 9612–8. doi:10.1021/bi980708e. PMID 9657673.
Prakash B, Praefcke GJ, Renault L; et al. (2000). "Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins". Nature 403 (6769): 567–71. doi:10.1038/35000617. PMID 10676968.
Zeng Q, Si X, Horstmann H; et al. (2000). "Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome". J. Biol. Chem. 275 (28): 21444–52. doi:10.1074/jbc.M000453200. PMID 10747914.
Ashar HR, James L, Gray K; et al. (2000). "Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules". J. Biol. Chem. 275 (39): 30451–7. doi:10.1074/jbc.M003469200. PMID 10852915.
Guenzi E, Töpolt K, Cornali E; et al. (2001). "The helical domain of GBP-1 mediates the inhibition of endothelial cell proliferation by inflammatory cytokines". EMBO J. 20 (20): 5568–77. doi:10.1093/emboj/20.20.5568. PMC 125279. PMID 11598000.
Long SB, Hancock PJ, Kral AM; et al. (2001). "The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics". Proc. Natl. Acad. Sci. U.S.A. 98 (23): 12948–53. doi:10.1073/pnas.241407898. PMC 60805. PMID 11687658.
Lobell RB, Omer CA, Abrams MT; et al. (2002). "Evaluation of farnesyl:protein transferase and geranylgeranyl:protein transferase inhibitor combinations in preclinical models". Cancer Res. 61 (24): 8758–68. PMID 11751396.
Bell IM, Gallicchio SN, Abrams M; et al. (2002). "3-Aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency". J. Med. Chem. 45 (12): 2388–409. doi:10.1021/jm010531d. PMID 12036349.
Long SB, Casey PJ, Beese LS (2002). "Reaction path of protein farnesyltransferase at atomic resolution". Nature 419 (6907): 645–50. doi:10.1038/nature00986. PMID 12374986.
Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
deSolms SJ, Ciccarone TM, MacTough SC; et al. (2003). "Dual protein farnesyltransferase-geranylgeranyltransferase-I inhibitors as potential cancer chemotherapeutic agents". J. Med. Chem. 46 (14): 2973–84. doi:10.1021/jm020587n. PMID 12825937.

PDB gallery

1d8d: CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION

1d8e: Zinc-depleted FTase complexed with K-RAS4B peptide substrate and FPP analog.

1fpp: PROTEIN FARNESYLTRANSFERASE COMPLEX WITH FARNESYL DIPHOSPHATE

1ft1: CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION

1ft2: CO-CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYL DIPHOSPHATE SUBSTRATE

1jcq: CRYSTAL STRUCTURE OF HUMAN PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYL DIPHOSPHATE AND THE PEPTIDOMIMETIC INHIBITOR L-739,750

1jcr: CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE NON-SUBSTRATE TETRAPEPTIDE INHIBITOR CVFM AND FARNESYL DIPHOSPHATE SUBSTRATE

1jcs: CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE PEPTIDE SUBSTRATE TKCVFM AND AN ANALOG OF FARNESYL DIPHOSPHATE

1kzo: PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY

1kzp: PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYLATED K-RAS4B PEPTIDE PRODUCT

1ld7: Co-crystal structure of Human Farnesyltransferase with farnesyldiphosphate and inhibitor compound 66

1ld8: Co-crystal structure of Human Farnesyltransferase with farnesyldiphosphate and inhibitor compound 49

1mzc: Co-Crystal Structure Of Human Farnesyltransferase With Farnesyldiphosphate and Inhibitor Compound 33a

1n94: Aryl Tetrahydropyridine Inhbitors of Farnesyltransferase: Glycine, Phenylalanine and Histidine Derivates

1n95: Aryl Tetrahydrophyridine Inhbitors of Farnesyltranferase: Glycine, Phenylalanine and Histidine Derivatives

1n9a: Farnesyltransferase complex with tetrahydropyridine inhibitors

1ni1: Imidazole and cyanophenyl farnesyl transferase inhibitors

1nl4: Crystal Structure of Rat Farnesyl Transferase in Complex With A Potent Biphenyl Inhibitor

1o1r: Structure of FPT bound to GGPP

1o1s: Structure of FPT bound to isoprenoid analog 3b

1o1t: Structure of FPT bound to the CVIM-FPP product

1o5m: Structure of FPT bound to the inhibitor SCH66336

1qbq: STRUCTURE OF RAT FARNESYL PROTEIN TRANSFERASE COMPLEXED WITH A CVIM PEPTIDE AND ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID.

1s63: Human protein farnesyltransferase complexed with L-778,123 and FPP

1sa4: human protein farnesyltransferase complexed with FPP and R115777

1sa5: Rat protein farnesyltransferase complexed with FPP and BMS-214662

1tn6: Protein Farnesyltransferase Complexed with a Rap2a Peptide Substrate and a FPP Analog at 1.8A Resolution

1tn7: Protein Farnesyltransferase Complexed with a TC21 Peptide Substrate and a FPP Analog at 2.3A Resolution

1tn8: Protein Farnesyltransferase Complexed with a H-Ras Peptide Substrate and a FPP Analog at 2.25A Resolution

1x81: Farnesyl transferase structure of Jansen compound

2bed: Structure of FPT bound to inhibitor SCH207736

2f0y: Crystal Structure Of Human Protein Farnesyltransferase Complexed With Farnesyl Diphosphate and hydantoin derivative

2h6f: Protein Farnesyltransferase Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.5A Resolution

2h6g: W102T Protein Farnesyltransferase Mutant Complexed with a Geranylgeranylated DDPTASACVLS Peptide Product at 1.85A Resolution

2h6h: Y365F Protein Farnesyltransferase Mutant Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.8A

2h6i: W102T/Y365F Protein Farnesyltransferase Double Mutant Complexed with a Geranylgeranylated DDPTASACVLS Peptide Product at 3.0A

2iej: Human Protein Farnesyltransferase Complexed with Inhibitor Compound STN-48 And FPP Analog at 1.8A Resolution

This article is issued from Wikipedia - version of the Wednesday, May 06, 2015. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

FNTB

References

Further reading