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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Structure
The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).[3] The predominant structure is β-sheet.[4] Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.[5]
Calcium binding-site
[6]
PC interaction
PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.[5]
Function
Biomedical interest
CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.[5]
Structural highlights
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- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:https://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ https://www.uniprot.org/uniprot/P02741
- ↑ https://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf
- ↑ 5.0 5.1 5.2 Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.
- ↑ Kumar, S. V., Ravunny, R. K., Chakraborty, C. (2011), Conserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP), Appl Biochem Biotechnol, 165:497–505