Abstract:
:A key step in the elimination of pathogens from the body is the covalent binding of complement proteins C3 and C4 to their surfaces. Proteolytic activation of these proteins results in a conformational change, and an internal thioester is exposed which reacts with amino or hydroxyl groups on the target surface to form amide or ester bonds, or is hydrolysed. We report here that the binding of the human C4A isotype involves a direct reaction between amino-nucleophiles and the thioester. A two-step mechanism is used by the C4B isotype. The histidine at position 1,106(aspartic acid in C4A) first attacks the thioester to form an acyl-imidazole intermediate. The released thiol then acts as a base to catalyse the transfer of the acyl group to amino- and hydroxyl-nucleophiles, including water.
journal_name
Naturejournal_title
Natureauthors
Dodds AW,Ren XD,Willis AC,Law SKdoi
10.1038/379177a0subject
Has Abstractpub_date
1996-01-11 00:00:00pages
177-9issue
6561eissn
0028-0836issn
1476-4687journal_volume
379pub_type
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