Structure, function and significance of Rh proteins in red cells.
OBJECTIVE
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.


RESULTS
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.


CONCLUSIONS
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.
Burton
Nicholas M
NM
Department of Biochemistry, University of Bristol and Bristol Institute for Transfusion Sciences, National Blood Service, Bristol, UK.
Anstee
David J
DJ
D004912:Erythrocytes / Q000378:metabolism*; D005260:Female; D006801:Humans; D007231:Infant, Newborn; D008958:Models, Molecular; D043370:Nitrosomonas europaea / Q000378:metabolism; D011247:Pregnancy; D012204:Rh-Hr Blood-Group System / Q000097:blood* / Q000737:chemistry; D013329:Structure-Activity Relationship
C066468:RHCE protein, human; D012204:Rh-Hr Blood-Group System; C026410:Rho(D) antigen