红细胞中Rh蛋白的结构、功能及意义
Structure, function and significance of Rh proteins in red cells.
作者信息
Burton Nicholas M, Anstee David J
机构信息
Department of Biochemistry, University of Bristol and Bristol Institute for Transfusion Sciences, National Blood Service, Bristol, UK.
出版信息
Curr Opin Hematol. 2008 Nov;15(6):625-30. doi: 10.1097/MOH.0b013e328311f422.
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.
综述目的
本文回顾了关于Rh相关糖蛋白（RhAG）结构和功能的最新数据，并探讨了从这些数据中能推断出的D和CE多肽的结构及功能意义。
最新发现
已解析出一种细菌RhAG（来自欧洲亚硝化单胞菌）的结构，并阐明了其气体通道。这些信息使我们能够构建比以往更精确的RhD和RhCE多肽结构模型。已证明人类RhAG可作为二氧化碳的气体通道。
总结
细菌RhAG结构的解析使我们能够比以往更精确地构建D和CE多肽的结构模型。结果表明，虽然RhAG有一个用于中性气体（二氧化碳、氨气，可能还有氧气和一氧化氮）通过的通道，但D和CE多肽不太可能具有转运功能。
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