2LTA

Solution NMR structure of De novo designed protein, rossmann 3x1 fold, Northeast Structural Genomics Consortium target OR157

2LTA の概要

• エントリーDOI: 10.2210/pdb2lta/pdb
• NMR情報: BMRB: 18465
• 分子名称: De novo designed protein (1 entity in total)
• 機能のキーワード: structural genomics, northeast structural genomics consortium, nesg, psi-biology, protein structure initiative, 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: 13065.00

構造登録者

Liu, G.,Koga, R.,Koga, N.,Xiao, R.,Pederson, K.,Hamilton, K.,Kohan, E.,Acton, T.B.,Kornhaber, G.,Everett, J.K.,Baker, D.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (登録日: 2012-05-15, 公開日: 2012-06-13, 最終更新日: 2024-05-15)

主引用文献

Koga, N.,Tatsumi-Koga, R.,Liu, G.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Baker, D.
Principles for designing ideal protein structures.
Nature, 491:222-227, 2012

PubMed Abstract: Unlike random heteropolymers, natural proteins fold into unique ordered structures. Understanding how these are encoded in amino-acid sequences is complicated by energetically unfavourable non-ideal features--for example kinked α-helices, bulged β-strands, strained loops and buried polar groups--that arise in proteins from evolutionary selection for biological function or from neutral drift. Here we describe an approach to designing ideal protein structures stabilized by completely consistent local and non-local interactions. The approach is based on a set of rules relating secondary structure patterns to protein tertiary motifs, which make possible the design of funnel-shaped protein folding energy landscapes leading into the target folded state. Guided by these rules, we designed sequences predicted to fold into ideal protein structures consisting of α-helices, β-strands and minimal loops. Designs for five different topologies were found to be monomeric and very stable and to adopt structures in solution nearly identical to the computational models. These results illuminate how the folding funnels of natural proteins arise and provide the foundation for engineering a new generation of functional proteins free from natural evolution.

PubMed: 23135467
DOI: 10.1038/nature11600

実験手法

SOLUTION NMR