Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).

@article{Aleshin2012StructureOC,
  title={Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).},
  author={Alexander E. Aleshin and Ingrid U. Schraufstatter and Boguslaw Stec and Laurie A. Bankston and Robert C. Liddington and Richard G. Discipio},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 13},
  pages={10210-22}
}
The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9. Together these form a lytic pore in bacterial membranes. C6 through C9 comprise a MAC-perforin domain flanked by 4-9 "auxiliary" domains. Here, we report the crystal structure of C6, the first and longest of the pore proteins to be recruited by C5b. Comparisons with the structures of the C8αβγ heterodimer and… CONTINUE READING

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Structure of complement C6 suggests a mechanism for initiation and unidirectional , sequential assembly of membrane attack complex ( MAC ) .
Structure of complement C6 suggests a mechanism for initiation and unidirectional , sequential assembly of membrane attack complex ( MAC ) .
Structure of complement C6 suggests a mechanism for initiation and unidirectional , sequential assembly of membrane attack complex ( MAC ) .
Structure of complement C6 suggests a mechanism for initiation and unidirectional , sequential assembly of membrane attack complex ( MAC ) .
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