期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1818, 期 4, 页码 1115-1122出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2011.07.046
关键词
Disease; Missense mutation; Membrane protein misfolding; Helix-helix interaction; Pharmacoperone; Folding
资金
- Canadian Institutes of Health Research (CIHR) [FRN-5810]
- Hospital for Sick Children
Helix-helix interactions play a central role in the folding and assembly of integral alpha-helical membrane proteins and are fundamentally dictated by the amino acid sequence of the TM domain. It is not surprising then that missense mutations that target these residues are often linked to disease. In this review, we focus on the molecular mechanisms through which missense mutations lead to aberrant folding and/or assembly of these proteins, and then discuss pharmacological approaches that may potentially mitigate or reverse the negative effects of these mutations. Improving our understanding of how missense mutations affect the interactions between TM alpha-helices will increase our capability to develop effective therapeutic approaches to counter the misassembly of these proteins and, ultimately, disease. This article is part of a Special Issue entitled: Protein Folding in Membranes. (C) 2011 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据