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1E0M

PROTOTYPE WW domain

1E0M の概要
エントリーDOI10.2210/pdb1e0m/pdb
関連するPDBエントリー1E0L 1E0N
分子名称WWPROTOTYPE (1 entity in total)
機能のキーワードsh3 prototype, wwprototype, protein design, de novo protein
由来する生物種SYNTHETIC CONSTRUCT
タンパク質・核酸の鎖数1
化学式量合計4358.74
構造登録者
Macias, M.J.,Gervais, V.,Civera, C.,Oschkinat, H. (登録日: 2000-04-01, 公開日: 2000-04-20, 最終更新日: 2024-05-15)
主引用文献Macias, M.J.,Gervais, V.,Civera, C.,Oschkinat, H.
Structural Analysis of Ww Domains and Design of a Ww Prototype
Nat.Struct.Biol., 7:375-, 2000
Cited by
PubMed Abstract: Two new NMR structures of WW domains, the mouse formin binding protein and a putative 84.5 kDa protein from Saccharomyces cerevisiae, show that this domain, only 35 amino acids in length, defines the smallest monomeric triple-stranded antiparallel beta-sheet protein domain that is stable in the absence of disulfide bonds, tightly bound ions or ligands. The structural roles of conserved residues have been studied using site-directed mutagenesis of both wild type domains. Crucial interactions responsible for the stability of the WW structure have been identified. Based on a network of highly conserved long range interactions across the beta-sheet structure that supports the WW fold and on a systematic analysis of conserved residues in the WW family, we have designed a folded prototype WW sequence.
PubMed: 10802733
DOI: 10.1038/75144
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 1e0m
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2024-11-13に公開中

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