Sandbox Reserved 1121: Difference between revisions
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=== CRP structure === | === CRP structure === | ||
Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/> | Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.<ref name="kumar"/> | ||
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 | 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> but short helical regions can be notice for residues 43 and 185.<ref name="kumar"/> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" /> | ||
=== Calcium binding-site === | === Calcium binding-site === | ||
<ref name="kumar">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</ref> | <ref name="kumar">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</ref> | ||
