Structure of C3b reveals conformational changes that underlie complement activity

Article Abstract:

The crystal structure of the activated complement protein C3b and the conformational rearrangements of the 12 domains that take place upon proteolytic activation are described. The structural data has indicated that the large conformational changes in the proteolytic activation and regulation of C3 take place mainly in the first conversion step, from C3 to C3b, which are important for the development of strategies to treat immune disorders that involve complement-mediated inflammation.

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The structure of complement C3b provides insights into complement activation and regulation

Article Abstract:

A structure of C3b is presented that reveals a marked loss of secondary structure in the CUB s domain, which together with the resulting translocation of the thioester domain provides a molecular basis for conformational changes accompanying the conversion of C3 to C3b. The covalently bound N-acetyl-L-threonine residue has demonstrated the geometry of C3b attachment to surface hydroxyl groups.

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