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1D8E

Zinc-depleted FTase complexed with K-RAS4B peptide substrate and FPP analog.

1D8E の概要
エントリーDOI10.2210/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
Long, S.B.,Casey, P.J.,Beese, L.S. (登録日: 1999-10-22, 公開日: 2000-03-20, 最終更新日: 2024-03-13)
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: 10673434
DOI: 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
Validation report summary of 1d8e
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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