1NL4

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

Summary for 1NL4

Entry DOI	10.2210/pdb1nl4/pdb
Descriptor	Protein farnesyltransferase alpha subunit, Protein farnesyltransferase beta subunit, ZINC ION, ... (5 entities in total)
Functional Keywords	transferase, prenyltransferase
Biological source	Rattus norvegicus (Norway rat) More
Total number of polymer chains	2
Total formula weight	83340.93
Authors	Curtin, M.L.,Florjancic, A.S.,Cohen, J.,Gu, W.-J.,Frost, D.J.,Muchmore, S.W.,Sham, H.L. (deposition date: 2003-01-06, release date: 2003-02-11, Last modification date: 2024-02-14)
Primary citation	Curtin, M.L.,Florjancic, A.S.,Cohen, J.,Gu, W.-J.,Frost, D.J.,Muchmore, S.W.,Sham, H.L. Novel and Selective Imidazole-containing Biphenyl Inhibitors of Protein Farnesyltransferase BIOORG.MED.CHEM.LETT., 13:1367-1371, 2003 Cited by PubMed Abstract: 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 (PubMed: 12657284 DOI: 10.1016/S0960-894X(03)00096-9 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation