title: Structure, function and significance of Rh proteins in red cells.
abstract: 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.
authors.affiliation: Department of Biochemistry, University of Bristol and Bristol Institute for Transfusion Sciences, National Blood Service, Bristol, UK.
authors.forename: Nicholas M
authors.initials: NM
authors.lastname: Burton
authors.forename: David J
authors.initials: DJ
authors.lastname: Anstee
mesh_terms: 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
chemical_list: C066468:RHCE protein, human; D012204:Rh-Hr Blood-Group System; C026410:Rho(D) antigen