title: NH2-terminal calcium-binding domain of human complement C1s- mediates the interaction of C1r- with C1q.
abstract: The assembly of C1, the first component of human complement, involves interactions between various domains of each of its three subcomponents, C1q, C1r, and C1s. The isolation, assignment of function, and structural characterization of the individual domains of C1r and C1s are critical for a thorough understanding of this complex assembly. The present study describes a 27-kDa plasmin-generated fragment derived from the NH2-terminal half of the heavy A chain of C1s-, the activated form of C1s. This fragment, C1s-alpha, was shown in the presence of Ca2+ to mimic the ability of whole C1s- to self-associate, bind to C1r-, and facilitate the binding of C1r to C1q. These results directly prove that the Ca2(+)-binding sites of C1s as well as all of the determinants necessary for binding of C1s- to C1r- and C1q are located in the NH2-terminal 27-kDa alpha region of the A chain.
authors.affiliation: Biochemistry Laboratory, American Red Cross Biomedical Research and Development, Rockville, Maryland 20855.
authors.forename: T F
authors.initials: TF
authors.lastname: Busby
authors.forename: K C
authors.initials: KC
authors.lastname: Ingham
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D003172:Complement C1 / Q000378:metabolism*; D015922:Complement C1q / Q000378:metabolism; D015923:Complement C1r / Q000378:metabolism; D003173:Complement C1s / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D003172:Complement C1; D010446:Peptide Fragments; D015922:Complement C1q; D015923:Complement C1r; D003173:Complement C1s; D002118:Calcium