ロード中...

The R163K Mutant of Human Thymidylate Synthase Is Stabilized in an Active Conformation: Structural Asymmetry and Reactivity of Cysteine 195

Loop 181-197 of human thymidylate synthase (hTS) populates two conformational states. In the first state, Cys195, a residue crucial for catalytic activity, is in the active site (active conformer); in the other conformation, it is about 10 Å away, outside the active site (inactive conformer). We hav...

詳細記述

保存先:
書誌詳細
主要な著者: Gibson, Lydia M., Lovelace, Leslie L., Lebioda, Lukasz
フォーマット: Artigo
言語:Inglês
出版事項: 2008
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC2575808/
https://ncbi.nlm.nih.gov/pubmed/18370400
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi7019386
タグ: タグ追加
タグなし, このレコードへの初めてのタグを付けませんか!