Computational design of ligand-binding proteins

被引:31
|
作者
Yang, Wei [1 ,2 ,3 ,4 ]
Lai, Luhua [1 ,2 ,3 ]
机构
[1] Peking Univ, BNLMS, State Key Lab Struct Chem Unstable & Stable Speci, Beijing 100871, Peoples R China
[2] Peking Univ, Coll Chem & Mol Engn, Peking Tsinghua Ctr Life Sci, Beijing 100871, Peoples R China
[3] Peking Univ, Ctr Quantitat Biol, Beijing 100871, Peoples R China
[4] Tsinghua Univ, Sch Life Sci, Beijing 100084, Peoples R China
基金
中国国家自然科学基金;
关键词
ENZYME DESIGN; TRANSCRIPTION FACTORS; MOLECULAR-DYNAMICS; HIGH-AFFINITY; DOCKING; SPECIFICITY; SELECTIVITY; TARGETS; SITES;
D O I
10.1016/j.sbi.2016.11.021
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Custom-designed ligand-binding proteins with novel functions hold the potential for numerous applications. In recent years, the developments of computational methods together with high-throughput experimental screening techniques have led to the generation of novel, high-affinity ligand-binding proteins for given ligands. In addition, naturally occurring ligand-binding proteins have been computationally designed to recognize new ligands while keeping their original biological functions at the same time. Furthermore, metalloproteins have been successfully designed for novel functions and applications. Though much has been learned in these successful design cases, advances in our understanding of protein dynamics and functions related to ligand binding and development of novel computational strategies are necessary to further increase the success rate of computational protein-ligand binding design.
引用
收藏
页码:67 / 73
页数:7
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