Topology and organization of human Rh (rhesus) blood group-related polypeptides.
J Biol Chem
; 269(9): 6417-23, 1994 Mar 04.
Article
em En
| MEDLINE
| ID: mdl-8119991
ABSTRACT
The Rh blood group antigens are associated with nonglycosylated human erythrocyte membrane proteins of molecular mass 30 kDa (the Rh30 polypeptides) and a glycoprotein of 40-100 kDa (the Rh glycoprotein). We have studied the topology of this family of proteins in the erythrocyte membrane. We confirmed the predicted cytosolic localization of the C and N termini of the Rh protein family. We located Lys-196 and Arg-323 of the Rh glycoprotein to the cytosol, and Glu-34 to the extracellular side of the plasma membrane in erythrocytes, by N-terminal sequencing of Rh glycoprotein peptides produced by proteolysis at the cytoplasmic or extracellular side of the membrane. We also show that a glycan chain is present on only one (Asn-37) of the three potential N-glycan addition sites in the Rh glycoprotein. Studies of the Rh glycoprotein fragments that co-immunoprecipitated with the Rh30 polypeptides suggest there is an interaction between the Rh30 polypeptides and amino acids 35-196 of the Rh glycoprotein. A model for the organization of the components of the Rh complex in the red cell membrane is proposed.
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Base de dados:
MEDLINE
Assunto principal:
Sistema do Grupo Sanguíneo Rh-Hr
/
Estrutura Secundária de Proteína
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
1994
Tipo de documento:
Article