Sandbox Reserved 1121: Difference between revisions
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== Structure == | == 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). <ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> | 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).<ref>http://www.uniprot.org/uniprot/P02741</ref> The predominant structure is β-sheet.<ref>http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf</ref> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /> | ||
=== Calcium binding-site === | === Calcium binding-site === | ||
