1rtk
From Proteopedia
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, resolution 2.30Å | |||||||
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Ligands: | , , , | ||||||
Gene: | BF (Homo sapiens) | ||||||
Activity: | Alternative-complement-pathway C3/C5 convertase, with EC number 3.4.21.47 | ||||||
Related: | 1RRK, 1RS0
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure Analysis of the Bb segment of Factor B complexed with 4-guanidinobenzoic acid
Contents |
Overview
The C-terminal fragment, Bb, of factor B combines with C3b to form the pivotal C3-convertase, C3bBb, of alternative complement pathway. Bb consists of a von Willebrand factor type A (vWFA) domain that is structurally similar to the I domains of integrins and a serine protease (SP) domain that is in inactive conformation. The structure of the C3bBb complex would be important in deciphering the activation mechanism of the SP domain. However, C3bBb is labile and not amenable to X-ray diffraction studies. We engineered a disulfide bond in the vWFA domain of Bb homologous to that shown to lock I domains in active conformation. The crystal structures of Bb(C428-C435) and its inhibitor complexes reveal that the adoption of the "active" conformation by the vWFA domain is not sufficient to activate the C3-convertase catalytic apparatus and also provide insights into the possible mode of C3-convertase activation.
Disease
Known disease associated with this structure: Macular degeneration, age-related, reduced risk of OMIM:[138470]
About this Structure
1RTK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase., Ponnuraj K, Xu Y, Macon K, Moore D, Volanakis JE, Narayana SV, Mol Cell. 2004 Apr 9;14(1):17-28. PMID:15068800
Page seeded by OCA on Sun Mar 30 23:32:47 2008