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2L42

The solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae

2L42 の概要
エントリーDOI10.2210/pdb2l42/pdb
分子名称DNA-binding protein RAP1 (1 entity in total)
機能のキーワードrap1, brct domain, dna binding protein, protein binding
由来する生物種Saccharomyces cerevisiae (yeast)
細胞内の位置Nucleus: P11938
タンパク質・核酸の鎖数1
化学式量合計12185.60
構造登録者
Zhang, W.,Zhang, J.,Tu, X. (登録日: 2010-09-29, 公開日: 2011-01-26, 最終更新日: 2024-05-01)
主引用文献Zhang, W.,Zhang, J.,Zhang, X.,Xu, C.,Tu, X.
Solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae reveals a novel fold
Biochem.Biophys.Res.Commun., 404:1055-1059, 2011
Cited by
PubMed Abstract: Rap1 (repressor-activator protein 1) from Saccharomyces cerevisiae, containing a BRCT domain at its N-terminus, is a multifunctional protein that controls telomere function, silencing, and the activation of glycolytic and ribosomal protein genes. In this work, we determined the solution structure of Rap1 BRCT domain, which contains three β-strands and three α-helices. Structural comparison indicated that Rap1 BRCT domain adopts a global fold similar to other BRCT domains, implying some common structural aspects of BRCT domain family. On the other hand, Rap1 BRCT domain displays structural characteristics significantly different from other BRCT domains in that Rap1 BRCT domain adopts a rather flexible conformation with less secondary structure elements, revealing a novel fold of the BRCT domain family.
PubMed: 21187076
DOI: 10.1016/j.bbrc.2010.12.109
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2l42
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2026-02-04に公開中

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