4FGT

Allosteric peptidic inhibitor of human thymidylate synthase that stabilizes inactive conformation of the enzyme.

4FGT の概要

• エントリーDOI: 10.2210/pdb4fgt/pdb
• 関連するPDBエントリー: 3EGY 3N5E
• 分子名称: Thymidylate synthase, CG peptide, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: dimer, mutant k47a of hts, inactive hts conformation, hts complex with peptidic inhibitor, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus : P04818
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38076.39

構造登録者

Tochowicz, A.,Finer-Moore, J.,Stroud, R.M.,Costi, M.P. (登録日: 2012-06-04, 公開日: 2013-03-06, 最終更新日: 2024-11-27)

主引用文献

Tochowicz, A.,Santucci, M.,Saxena, P.,Guaitoli, G.,Trande, M.,Finer-Moore, J.,Stroud, R.M.,Costi, M.P.
Alanine mutants of the interface residues of human thymidylate synthase decode key features of the binding mode of allosteric anticancer peptides.
J.Med.Chem., 58:1012-1018, 2015

PubMed Abstract: Allosteric peptide inhibitors of thymidylate synthase (hTS) bind to the dimer interface and stabilize the inactive form of the protein. Four interface residues were mutated to alanine, and interaction studies were employed to decode the key role of these residues in the peptide molecular recognition. This led to the identification of three crucial interface residues F59, L198, and Y202 that impart activity to the peptide inhibitors and suggest the binding area for further inhibitor design.

PubMed: 25427005
DOI: 10.1021/jm5011176

実験手法

X-RAY DIFFRACTION (2 Å)