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Polymorphism of structural forms of C-reactive protein
Hong-Wei Wang1, Yi Wu, Yong Chen
1Department of Biological Sciences and Biotechnology, State-Key Laboratory of Biomembranes, Tsinghua University, Beijing 100084, P.R. China.
International Journal of Molecular Medicine
|May 16, 2002
Summary
C-reactive protein (CRP) exhibits diverse structures, including pentameric, globulin-like, and novel fibril forms, on membranes. These structural variations may explain CRP's multiple physiological functions.
Area of Science:
- Biochemistry
- Structural Biology
- Immunology
Background:
- C-reactive protein (CRP) is a key acute-phase reactant.
- CRP has diverse physiological roles in vivo and in vitro.
- The structural basis for CRP's varied functions is not fully understood.
Purpose of the Study:
- To investigate the different structural forms of CRP.
- To characterize CRP structures in solution and on phospholipid membranes.
- To explore the relationship between CRP structure and function.
Main Methods:
- Size-exclusion chromatography
- Electron microscopy
- Phospholipid membrane interaction studies
- Calcium dependency assays
Main Results:
- Identified three CRP structures: pentameric, globulin-like, and fibril-like.
- Pentameric CRP binds to ligand-containing membranes in a calcium-dependent manner.
- Globulin-like CRP monomers are stable on negatively charged membranes without calcium.
- Novel fibril-like structures formed by CRP pentamer stacking were observed, varying in length and bundling based on storage time.
Conclusions:
- CRP exists in multiple structural forms, including novel fibrils.
- Structural plasticity of CRP may underlie its diverse physiological functions.
- Interconversion between CRP forms under specific conditions is suggested.