Refined views of multi-protein complexes in the erythrocyte membrane

被引:55
|
作者
Mankelow, T. J. [2 ]
Satchwell, T. J. [1 ]
Burton, N. M. [1 ,2 ]
机构
[1] Univ Bristol, Sch Biochem, Bristol BS8 1TD, Avon, England
[2] NHS Blood & Transplant, Bristol Inst Transfus Sci, Bristol, Avon, England
基金
英国惠康基金;
关键词
Band; 3; Ankyrin; Protein; 4.1R; Macrocomplex; Junctional complex; Protein modelling; SPECTRIN-ACTIN-BINDING; BLOOD-CELL MEMBRANE; HUMAN RED-CELLS; CYTOPLASMIC DOMAIN; GLYCOPHORIN-A; ANION-EXCHANGER; RH-DEFICIENCY; BAND; 4.2; STRUCTURAL ORGANIZATION; CRYSTAL-STRUCTURE;
D O I
10.1016/j.bcmd.2012.03.001
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
The erythrocyte membrane has been extensively studied, both as a model membrane system and to investigate its role in gas exchange and transport. Much is now known about the protein components of the membrane, how they are organised into large multi-protein complexes and how they interact with each other within these complexes. Many links between the membrane and the cytoskeleton have also been delineated and have been demonstrated to be crucial for maintaining the deformability and integrity of the erythrocyte. In this study we have refined previous, highly speculative molecular models of these complexes by including the available data pertaining to known protein-protein interactions. While the refined models remain highly speculative, they provide an evolving framework for visualisation of these important cellular structures at the atomic level. (C) 2012 Elsevier Inc. All rights reserved.
引用
收藏
页码:1 / 10
页数:10
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