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Structure, function and significance of Rh proteins in red cells
被引：24
|作者：
Burton, Nicholas M.
Anstee, David J.
[1
]
机构：
[1] Natl Blood Serv, Bristol Inst Transfus Sci, Bristol BS10 5ND, Avon, England
关键词：
band;
3;
macrocomplex;
carbon dioxide;
CE polypeptide;
D polypeptide;
gas metabolon;
haemolytic disease of the fetus and the newborn;
nitric oxide;
oxygen;
Rh-associated glycoprotein;
D O I：
10.1097/MOH.0b013e328311f422
中图分类号：
R5 [内科学];
学科分类号：
1002 ;
100201 ;
摘要：
Purpose of review The present article reviews recent data concerning the structure and function of the Rh-associated glycoprotein (RhAG) and considers what can be inferred about the structure and functional significance of the D and CE polypeptides. Recent findings The structure of a bacterial RhAG (from Nitrosomonas europaea) has been solved and its gas channel elucidated. This information allows us to model a more accurate structure of RhD and RhCE polypeptides than has been possible hitherto. Human RhAG has been shown to act as a gas channel for CO2. Summary Elucidation of the structure of a bacterial RhAG allows us to model the structure of D and CE polypeptides more accurately than before. Results suggest that whereas RhAG has a channel for passage of neutral gases (CO2, NH3 and possibly oxygen and nitric oxide), D and CE polypeptides are unlikely to have a transport function.
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页码：625 / 630
页数：6
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