折叠(高阶函数)
蛋白质结构
功能(生物学)
免疫球蛋白结构域
化学
生物
生物物理学
结晶学
抗体
遗传学
生物化学
计算机科学
程序设计语言
作者
Yanan He,Yihong Chen,Patrick Alexander,Philip N. Bryan,John Orban
出处
期刊:Structure
[Elsevier]
日期:2012-02-01
卷期号:20 (2): 283-291
被引量:98
标识
DOI:10.1016/j.str.2011.11.018
摘要
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.
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