Abstract:
: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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Ponnuraj K,Xu Y,Macon K,Moore D,Volanakis JE,Narayana SVdoi
10.1016/s1097-2765(04)00160-1subject
Has Abstractpub_date
2004-04-09 00:00:00pages
17-28issue
1eissn
1097-2765issn
1097-4164pii
S1097-2765(04)00160-1journal_volume
14pub_type
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