Hydrophobic cluster analysis reveals duplication in the external structure of human alpha-interferon receptor and homology with gamma-interferon receptor external domain.
Evidence is presented, based on sequence comparison according to Hydrophobic Cluster Analysis, of a structural and evolutionary relationship between the human alpha/beta-interferon receptor and the human and mouse gamma-interferon receptor. These results predict that the human alpha/beta-interferon receptor extracellular part is organised in two homologous subdomains connected by a proline linker. They also predict that both subdomains present some homologies to the external domain of mouse and human gamma interferon receptor.
Gaboriaud
C
C
Laboratoire de Minéralogie-Cristallographie, CNRS U A09, Université P6, France.
Uzé
G
G
Lutfalla
G
G
Mogensen
K
K
D000595:Amino Acid Sequence; D005110:Extracellular Space; D006801:Humans; D008565:Membrane Proteins / Q000648:ultrastructure*; D008969:Molecular Sequence Data; D011971:Receptors, Immunologic / Q000648:ultrastructure*; D017471:Receptors, Interferon
D008565:Membrane Proteins; D011971:Receptors, Immunologic; D017471:Receptors, Interferon