Convergent and divergent mechanisms of sugar recognition across kingdoms

被引:60
作者
Taylor, Maureen E. [1 ]
Drickamer, Kurt [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Dept Life Sci, London SW7 2AZ, England
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
HOMOLOGY MRH DOMAIN; STRUCTURAL BASIS; CARBOHYDRATE-BINDING; LIGAND-BINDING; ENDOPLASMIC-RETICULUM; MOLECULAR-BASIS; QUALITY-CONTROL; PA14; DOMAIN; DC-SIGN; LECTIN;
D O I
10.1016/j.sbi.2014.07.003
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
Protein modules that bind specific oligosaccharides are found across all kingdoms of life from single-celled organisms to man. Different, overlapping and evolving designations for sugarbinding domains in proteins can sometimes obscure common features that often reflect convergent solutions to the problem of distinguishing sugars with closely similar structures and binding them with sufficient affinity to achieve biologically meaningful results. Structural and functional analysis has revealed striking parallels between protein domains with widely different structures and evolutionary histories that employ common solutions to the sugar recognition problem. Recent studies also demonstrate that domains descended from common ancestors through divergent evolution appear more widely across the kingdoms of life than had previously been recognized.
引用
收藏
页码:14 / 22
页数:9
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