Conformation and restricted segmental flexibility of C1, the first component of human complement.
Seventy selected images of chemically crosslinked C1 are analyzed to illustrate structural details of the C1qC1r2C1s2 complex. From inspection of these images, the C1r2C1s2 tetramer can be seen to be located in the region of the C1q arms, cleanly separated from the C1q heads and from at least 90%, if not all, of the C1q stem. From measurements made upon 65 images, the semicone angles formed between the spreading arms and the symmetry axis passing through the stem of C1 may be calculated. Unlike C1q, for which a wide variety of angles is found, the C1 complex appears to possess a restricted range of angular flexibility with an average value of about 50 degrees. The volume inside the cone formed by the spreading arms of C1q is too small to contain the entire C1r2C1s2 tetramer; at least some of the tetramer must lie outside the cone when it is bound to C1q to form C1. From our knowledge of the sizes and structures of its subunits, and from symmetry considerations, a model is proposed for the configuration of the C1 complex in which the middle portion of the C1r2C1s2 tetramer is centrally located among the arms close to the stem of the C1q and with the two protruding ends of the tetramer wrapped around the outside of the cone. Functional implications of this more rigid structure are discussed with relevance to C1q-induced aggregation of latex beads and C1-induced disaggregation.
D003166:Complement Activating Enzymes; D003172:Complement C1; D015922:Complement C1q; D015923:Complement C1r; D003173:Complement C1s; D006801:Humans; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008958:Models, Molecular; D011487:Protein Conformation
D003172:Complement C1; D046911:Macromolecular Substances; D015922:Complement C1q; D003166:Complement Activating Enzymes; D015923:Complement C1r; D003173:Complement C1s