Molecular nature of the complement lesion. | Zendy

Sucharit Bhakdi | Zendy; J Tranum-Jensen | Zendy

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Molecular nature of the complement lesion.

Author(s) -

Sucharit Bhakdi,

J Tranum-Jensen

Publication year - 1978

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.75.11.5655

Subject(s) - macromolecule , lipid bilayer , biophysics , membrane , complement system , vesicle , chemistry , transmembrane protein , complement component 5 , complement membrane attack complex , complement (music) , bilayer , biochemistry , microbiology and biotechnology , biology , receptor , antibody , immunology , complementation , gene , phenotype

The principle molecular event leading to membrane perturbation by complement is the assembly of the terminal five serum complement components (C5b-C9) into a macromolecular C5b-9 complex on the target membrane [Müller-Eberhard, H.-J. (1975) Ann. Rev. Biochem. 44, 697--723]. The present communication reports on the ability of purified C5b-9 complexes isolated from target membranes to become reincorporated into artificial lipid vesicles. The data indicate that the complex is a vertically oriented, hollow, cylindrical macromolecule possessing lipid-binding regions that enable one terminus to penetrate into the lipid bilayer. A transmembrane pore appears to be created at the attachment site of the C5b-9 complex.

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