1dle
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FACTOR B SERINE PROTEASE DOMAIN
OverviewOverview
Factor B and C2 are two central enzymes for complement activation. They, are multidomain serine proteases and require cofactor binding for full, expression of proteolytic activities. We present a 2.1 A crystal structure, of the serine protease domain of factor B. It shows a number of structural, motifs novel to the chymotrypsin fold, which by sequence homology are, probably present in C2 as well. These motifs distribute characteristically, on the protein surface. Six loops surround the active site, four of which, shape substrate-binding pockets. Three loops next to the oxyanion hole, which typically mediate zymogen activation, are much shorter or absent., Three insertions including the linker to the preceding domain bulge from, the side opposite to the active site. The catalytic triad and non-specific, substrate-binding site display active conformations, but the oxyanion hole, displays a zymogen-like conformation. The bottom of the S1 pocket has a, negative charge at residue 226 instead of the typical 189 position. These, unique structural features may play different roles in domain-domain, interaction, cofactor binding and substrate binding.
DiseaseDisease
Known diseases associated with this structure: Macular degeneration, age-related, reduced risk of OMIM:[138470]
About this StructureAbout this Structure
1DLE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
New structural motifs on the chymotrypsin fold and their potential roles in complement factor B., Jing H, Xu Y, Carson M, Moore D, Macon KJ, Volanakis JE, Narayana SV, EMBO J. 2000 Jan 17;19(2):164-73. PMID:10637221
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