Annual Review of Immunology Volume 5 1987 by The Annual Reviews

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In order to form a symmetrical structure from two objects that possess sixfold and twofold symmetries, it is necessary that the axes of symmetrybe madeto coincide ; thus, the only way that symmetrycan be maintained and the tetramer be positioned between the stem and heads of Clq is if the Clrz portion is aligned symmetrically within the cone formed by the spreading Clq arms. Then the protruding ends of the tetramer must be folded around or within the cone to form an S-shaped structure. In the symmetrical model proposed by Poon et al (65), Schumakeret al (3), and Weiss et al (27), the protruding ends are wrapped around the outside of the cone (Figures 1B,C).

Physiochemical and functional characterization of the Clr subunit of the first Annual Reviews Annu. Rev. Immunol. 5:21-42. org by HINARI on 08/28/07. For personal use only. 40 SCHUMAKER, ZAVODSZKY & POON complement component. J. Immunol. 116 : 496-503 34. Ziccardi, R. , Cooper, N. R. 1976. Activation of C 1 r by proteolytic cleavage. J. Immunol. 116:504-9 35. Arlaud, (3. , Villiers, C. , Colomb,M. G. 1980. Purified proenzymeC1 r. Somecharacteristics of its activation and subsequent proteolytic cleavage.

Rev. Immunol. 5:21-42. org by HINARI on 08/28/07. For personal use only. chain to the center of the tetramer (Figure 1A; 27). This identification of the interaction domainsis compatible with the results of proteolytic fragmentation studies, which show that the isolated catalytic domains of Cls or Clr2 will not associate with the other subcomponent(35a). The electron microscope studies of the tetrameter have led to the conclusion (9, 41, 65) that Clr2Cls2 possessed an axis of two-fold rotational symmetry, since manyof the molecules showed an inverted S-shape on the carbon support.

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