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Structure paper

TitleCrystal Structures of the Anticancer Clinical Candidates R115777 (Tipifarnib) and BMS-214662 Complexed with Protein Farnesyltransferase Suggest a Mechanism of FTI Selectivity.
Journal, issue, pagesBiochemistry, Vol. 43, Page 6877-6884, Year 2004
Publish dateFeb 6, 2004 (structure data deposition date)
AuthorsReid, T.S. / Beese, L.S.
External linksBiochemistry / PubMed:15170324
MethodsX-ray diffraction
Resolution2.1 - 2.6 Å
Structure data

PDB-1sa4:
human protein farnesyltransferase complexed with FPP and R115777
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1sa5:
Rat protein farnesyltransferase complexed with FPP and BMS-214662
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-FPP:
FARNESYL DIPHOSPHATE

ChemComp-JAN:
6-[(S)-AMINO(4-CHLOROPHENYL)(1-METHYL-1H-IMIDAZOL-5-YL)METHYL]-4-(3-CHLOROPHENYL)-1-METHYLQUINOLIN-2(1H)-ONE / inhibitor*YM

ChemComp-HOH:
WATER

ChemComp-BMV:
3-BENZYL-1-(1H-IMIDAZOL-4-YLMETHYL)-4-(THIEN-2-YLSULFONYL)-2,3,4,5-TETRAHYDRO-1H-1,4-BENZODIAZEPINE-7-CARBONITRILE

ChemComp-ACY:
ACETIC ACID

Source
  • homo sapiens (human)
  • rattus norvegicus (Norway rat)
KeywordsTRANSFERASE / FTASE / FARNESYLTRANSFERASE / FARNESYL TRANSFERASE / CAAX / RAS / CANCER / TUMOR REGRESSION / R115777 / TIPIFARNIB / ZARNESTRA / FTI / CLINICAL CANDIDATE / INHIBITOR / PROTEIN PRENYLATION / LIPID MODIFICATION / BMS-214662

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