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2LHG

GB98-T25I solution structure

2LHG の概要
エントリーDOI10.2210/pdb2lhg/pdb
関連するPDBエントリー2LHC 2LHD 2LHE
NMR情報BMRB: 17843
分子名称GB98 (1 entity in total)
機能のキーワードde novo protein
由来する生物種artificial gene
タンパク質・核酸の鎖数1
化学式量合計6417.42
構造登録者
He, Y.,Chen, Y.,Alexander, P.,Bryan, P.,Orban, J. (登録日: 2011-08-08, 公開日: 2012-02-29, 最終更新日: 2024-05-01)
主引用文献He, Y.,Chen, Y.,Alexander, P.A.,Bryan, P.N.,Orban, J.
Mutational tipping points for switching protein folds and functions.
Structure, 20:283-291, 2012
Cited by
PubMed Abstract: While disordered to ordered rearrangements are relatively common, the ability of proteins to switch from one ordered fold to a completely different fold is generally regarded as rare, and few fold switches have been characterized. Here, in a designed system, we examine the mutational requirements for transitioning between folds and functions. We show that switching between monomeric 3α and 4β+α folds can occur in multiple ways with successive single amino acid changes at diverse residue positions, raising the likelihood that such transitions occur in the evolution of new folds. Even mutations on the periphery of the core can tip the balance between alternatively folded states. Ligand-binding studies illustrate that a new immunoglobulin G-binding function can be gained well before the relevant 4β+α fold is appreciably populated in the unbound protein. The results provide new insights into the evolution of fold and function.
PubMed: 22325777
DOI: 10.1016/j.str.2011.11.018
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 2lhg
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2024-11-06に公開中

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