1qqf
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N-TERMINALLY TRUNCATED C3D,G FRAGMENT OF THE COMPLEMENT SYSTEM
OverviewOverview
Complement component C3 plays a key role in the complement-mediated immune, defence, and occupies a central position within the complement cascade, system. One of its degradation products, C3dg, was purified from rat serum, and crystallised in two different crystal forms as N-terminally truncated, fragment. Despite the truncation and the lack of a significant portion of, the N-terminus as compared to C3d, the structure of the fragment is highly, similar to that of recombinant human C3d (Nagar et al., Science 280 (1998), 1277-1281). Structural details of the reactive site have been obtained, suggesting a possible mode of thioester bond formation between Cys-1010, and Gln-1013 and thioester bond cleavage in the transacylation reaction, involving His-1126. The truncation at the N-terminus of C3d leads to the, exposure of a surface of the molecule that favours dimerisation, so that, in both crystal forms, the fragment is present as a dimer, with monomers, related by a two-fold axis.
About this StructureAbout this Structure
1QQF is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Structure at 1.44 A resolution of an N-terminally truncated form of the rat serum complement C3d fragment., Zanotti G, Bassetto A, Battistutta R, Folli C, Arcidiaco P, Stoppini M, Berni R, Biochim Biophys Acta. 2000 May 23;1478(2):232-8. PMID:10825534
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