1D8D

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

Summary for 1D8D

• Entry DOI: 10.2210/pdb1d8d/pdb
• Related: 1d8e 1ft1 1ft2
• Descriptor: farnesyltransferase (alpha subunit), farnesyltransferase (beta subunit), K-RAS4B PEPTIDE SUBSTRATE, ... (7 entities in total)
• Functional Keywords: ftase, pft, pftase, farnesyltransferase, farnesyl transferase, caax, ras, cancer, transferase
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cell membrane; Lipid-anchor; Cytoplasmic side: P01116
• Total number of polymer chains: 3
• Total formula weight: 94780.13

Authors

Long, S.B.,Casey, P.J.,Beese, L.S. (deposition date: 1999-10-22, release date: 2000-02-09, Last modification date: 2024-03-13)

Primary citation

Long, S.B.,Casey, P.J.,Beese, L.S.
The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures.
Structure Fold.Des., 8:209-222, 2000

PubMed Abstract: The protein farnesyltransferase (FTase) catalyzes addition of the hydrophobic farnesyl isoprenoid to a cysteine residue fourth from the C terminus of several protein acceptors that are essential for cellular signal transduction such as Ras and Rho. This addition is necessary for the biological function of the modified proteins. The majority of Ras-related human cancers are associated with oncogenic variants of K-RasB, which is the highest affinity natural substrate of FTase. Inhibition of FTase causes regression of Ras-mediated tumors in animal models.

PubMed: 10673434
DOI: 10.1016/S0969-2126(00)00096-4

Experimental method

X-RAY DIFFRACTION (2 Å)