1D8E
Zinc-depleted FTase complexed with K-RAS4B peptide substrate and FPP analog.
1D8E の概要
エントリーDOI | 10.2210/pdb1d8e/pdb |
関連するPDBエントリー | 1d8d 1ft1 1ft2 |
分子名称 | FARNESYLTRANSFERASE (ALPHA SUBUNIT), FARNESYLTRANSFERASE (BETA SUBUNIT), K-RAS4B PEPTIDE SUBSTRATE, ... (6 entities in total) |
機能のキーワード | ftase, pft, pftase, farnesyltransferase, farnesyl transferase, caax, ras, cancer, transferase |
由来する生物種 | Rattus norvegicus (Norway rat) 詳細 |
細胞内の位置 | Cell membrane; Lipid-anchor; Cytoplasmic side: P01116 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 94537.59 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 10673434DOI: 10.1016/S0969-2126(00)00096-4 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード