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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Burton et al. (2008) studied this question.
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