期刊
CURRENT OPINION IN HEMATOLOGY
卷 15, 期 6, 页码 625-630出版社
LIPPINCOTT WILLIAMS & WILKINS
DOI: 10.1097/MOH.0b013e328311f422
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
类别
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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