Loading...
Arranged sevenfold: structural insights into the C-terminal oligomerization domain of human C4b-binding protein.
Hofmeyer, Thomas Schmelz, Stefan Degiacomi, Matteo T Dal Peraro, Matteo Daneschdar, Matin Scrima, Andrea van den Heuvel, Joop Heinz, Dirk W
Hofmeyer, Thomas
Schmelz, Stefan
Degiacomi, Matteo T
Dal Peraro, Matteo
Daneschdar, Matin
Scrima, Andrea
van den Heuvel, Joop
Heinz, Dirk W
Citations
Altmetric:
Advisors
Editors
Other Contributors
Issue Date
2013-04-26
Submitted date
Files
Other Titles
Abstract
The complement system as a major part of innate immunity is the first line of defense against invading microorganisms. Orchestrated by more than 60 proteins, its major task is to discriminate between host cells and pathogens and to initiate immune response. Additional recognition of necrotic or apoptotic cells demands a fine-tune regulation of this powerful system. C4b-binding protein (C4BP) is the major inhibitor of the classical complement and lectin pathway. The crystal structure of the human C4BP oligomerization domain in its 7α isoform and molecular simulations provide first structural insights of C4BP oligomerization. The heptameric core structure is stabilized by intermolecular disulfide bonds. In addition, thermal shift assays indicate that layers of electrostatic interactions mainly contribute to the extraordinary thermodynamic stability of the complex. These findings make C4BP a promising scaffold for multivalent ligand display with applications in immunology and biological chemistry.
Citation
Arranged sevenfold: structural insights into the C-terminal oligomerization domain of human C4b-binding protein. 2013, 425 (8):1302-17 J. Mol. Biol.
Publisher
Journal
PubMed ID
PubMed Central ID
Additional Links
Embedded video
Type
Article
Language
en
Description
Series/Report no.
ISSN
1089-8638
EISSN
ISBN
ISMN
Gov't Doc #
Sponsors
License
Archived with thanks to Journal of molecular biology