Expression, crystallization and preliminary crystallographic analysis of C-reactive protein from zebrafish
- Authors
- Chen, R., Qi, J., Yao, S., Pan, X., Gao, F., and Xia, C.
- ID
- ZDB-PUB-111206-7
- Date
- 2011
- Source
- Acta crystallographica. Section F, Structural biology and crystallization communications 67: 12 (Journal)
- Registered Authors
- Keywords
- C-reactive protein, pentraxin, zebrafish
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- C-Reactive Protein/chemistry*
- C-Reactive Protein/genetics
- C-Reactive Protein/isolation & purification
- Crystallization
- Crystallography, X-Ray
- Gene Expression
- Humans
- Molecular Sequence Data
- Sequence Alignment
- Zebrafish*/genetics
- PubMed
- 22139185 Full text @ Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
C-reactive protein (CRP) is an acute phase protein that is found in blood, the concentration of which in plasma rises rapidly in response to inflammation. It functions as a pattern-recognition molecule, recognizing dead cells and various pathogenic agents and eliminating them by utilizing the classical complement pathway and activating macrophages. CRP is phylogenetically highly conserved in invertebrates and mammals. To date, information on the CRP gene has been reported from numerous species of animals, but little is known about the structure of CRP from species other than humans. In order to solve the structure of CRP from bony fish, the CRP gene from zebrafiah (Danio rerio) was cloned and expressed in Escherichia coli. The zebrafish CRP (Dare-CRP) was then purified and crystallized. The crystal diffracted to 2.3 Å resolution and belonged to space group R3, with unit-cell parameters a = b = 114.7, c = 61.0 Å. The Matthews coefficient and solvent content were calculated to be 3.28 Å3 Da-1 and 62.55%, respectively. Determination of the zebrafish CRP structure should be helpful in investigating the evolution of CRPs in the innate immune system.