2LHG
GB98-T25I solution structure
2LHG の概要
エントリーDOI | 10.2210/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: 22325777DOI: 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 |
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