Structure, function and significance of Rh proteins in red cells

被引：25

作者：

Burton, Nicholas M.

Anstee, David J. ^{[1
]}

机构：

[1] Natl Blood Serv, Bristol Inst Transfus Sci, Bristol BS10 5ND, Avon, England

来源：

CURRENT OPINION IN HEMATOLOGY | 2008年 / 15卷 / 06期

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.

引用

页码：625 / 630

页数：6

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