title: The structures of human C1r and C1s and their relationship to other serine proteases.
abstract: The recent sequencing of the C1 subcomponents has allowed comparison with other molecules of homologous primary structure. Where tertiary structures are available for at least one member of the family it is possible to make further progress by modelling the amino acid sequence of the complement protein into the three-dimensional coordinates of the directly determined structure, thereby obtaining an approximation of the structure of the complement protein. Molecular modelling allows structure-function relationships to be explored and suggests further experiments that may be amenable to techniques such as site-directed mutagenesis.
authors.affiliation: Department of Biochemistry, University of Aberdeen, Marischal College, U.K.
authors.forename: J
authors.initials: J
authors.lastname: Fothergill
authors.forename: G
authors.initials: G
authors.lastname: Kemp
authors.forename: N
authors.initials: N
authors.lastname: Paton
authors.forename: P
authors.initials: P
authors.lastname: Carter
authors.forename: P
authors.initials: P
authors.lastname: Gray
mesh_terms: D000595:Amino Acid Sequence; D015923:Complement C1r / Q000235:genetics; D003173:Complement C1s / Q000235:genetics; D006801:Humans; D008958:Models, Molecular; D015394:Molecular Structure; D005810:Multigene Family; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases / Q000235:genetics
chemical_list: D012697:Serine Endopeptidases; D015923:Complement C1r; D003173:Complement C1s