1FT1

CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25 ANGSTROMS RESOLUTION

1FT1 の概要

• エントリーDOI: 10.2210/pdb1ft1/pdb
• 分子名称: PROTEIN FARNESYLTRANSFERASE, ZINC ION, ... (4 entities in total)
• 機能のキーワード: cancer therapeutics, g proteins, prenyltransferase, signal transduction, ras, transferase
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92885.84

構造登録者

Beese, L.S.,Park, H.-W. (登録日: 1997-03-17, 公開日: 1998-03-18, 最終更新日: 2024-02-07)

主引用文献

Park, H.W.,Boduluri, S.R.,Moomaw, J.F.,Casey, P.J.,Beese, L.S.
Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution.
Science, 275:1800-1804, 1997

PubMed Abstract: Protein farnesyltransferase (FTase) catalyzes the carboxyl-terminal lipidation of Ras and several other cellular signal transduction proteins. The essential nature of this modification for proper function of these proteins has led to the emergence of FTase as a target for the development of new anticancer therapy. Inhibition of this enzyme suppresses the transformed phenotype in cultured cells and causes tumor regression in animal models. The crystal structure of heterodimeric mammalian FTase was determined at 2.25 angstrom resolution. The structure shows a combination of two unusual domains: a crescent-shaped seven-helical hairpin domain and an alpha-alpha barrel domain. The active site is formed by two clefts that intersect at a bound zinc ion. One cleft contains a nine-residue peptide that may mimic the binding of the Ras substrate; the other cleft is lined with highly conserved aromatic residues appropriate for binding the farnesyl isoprenoid with required specificity.

PubMed: 9065406
DOI: 10.1126/science.275.5307.1800

実験手法

X-RAY DIFFRACTION (2.25 Å)