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Intermodule cooperativity in the structure and dynamics of consecutive complement control modules in human C1r:
András Láng1, Katalin Szilágyi, Balázs Major
1Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Budapest, Hungary.
The FEBS Journal
|August 28, 2010
Summary
The C1r protein
Area of Science:
- Biochemistry
- Immunology
- Structural Biology
Background:
- The classical complement pathway initiates innate immunity via the C1 complex.
- C1r protease activation requires precise regulation of the C1 complex's flexibility and interactions.
Purpose of the Study:
- To investigate the structural dynamics and cooperativity of C1r's complement control protein (CCP) modules.
- To understand the role of CCP1 and CCP2 domains in C1r protein folding, stability, and dynamics.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy to determine solution structures and conformational dynamics.
- X-ray crystallography for structural comparison.
- Preparation of free CCP1, CCP2, and tandem CCP1CCP2 constructs.
Main Results:
- NMR and X-ray crystallography structures were consistent.
- Expression of CCP1 and CCP1CCP2 required the N-terminal CUB2 module.
- CCP1 dynamics and stability are significantly influenced by the adjacent CCP2 domain.
Conclusions:
- CCP1's folding, stability, and dynamics depend on neighboring modules within the intact C1r protein.
- CCP1 may act as a key interaction site, mediating information transfer within the C1r complex.
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