Structures of complement component C3 provide insights into the function and evolution of immunity

Article Abstract:

Crystal structures of native C3 and its final major proteolytic fragment C3c are presented. Marked conformational changes in the alpha-chain, including movement of a critical interaction site through a ring formed by the domains of the beta-chain, indicate an unprecedented, conformation-dependent mechanism of activation, regulation and biological function of C3.

Analysis, Domain structure, Proteomics

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Exposure of an executioner

Article Abstract:

The structure of the human native complement protein C3, the form of protein before activation, and the X-ray structures of C3b, the active form of human C3, is provided. The C3 protein is found to bind to pathogens, signaling them out for execution by the immune system.

Massachusetts, Health aspects, Diagnosis, Observations, C-reactive protein, X-ray crystallography, Macular degeneration

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Similar abstracts:

• Abstracts: Structure of C3b reveals conformational changes that underlie complement activity

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