Sandbox Reserved 1121: Difference between revisions

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=== 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"/>.

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 one α-helix and two antiparallel β-sheets <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 noticed for the residues 43 and 185 <ref name="kumar"/>. The residues Glu197 and Lys123 of CRP form an intermolecular ion pair <ref name="thompson" />.

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 one α-helix and two antiparallel β-sheets <ref>[http://www.uniprot.org/uniprot/P02741 "UniProtKB"]</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 noticed for the residues 43 and 185 <ref name="kumar"/>. The residues Glu197 and Lys123 of CRP form an intermolecular ion pair <ref name="thompson" />.

The diameter of the CRP pentamer is 102 Å, the inner pore diameter is 30 Å and the diameter of a subunit is 36 Å <ref name="agrawal">A. Agrawal, P. P. Singh, B. Bottazzi, C. Garlanda, A. Mantovani, Pattern recognition by Pentraxins, Adv Exp Med Biol. 2009; 653: 98-116</ref>.

=== Ca<sup>2+</sup> binding-site ===

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@@ Line 10: / Line 10: @@
 === 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"/>.
-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 one α-helix and two antiparallel β-sheets <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 noticed for the residues 43 and 185 <ref name="kumar"/>. The residues Glu197 and Lys123 of CRP form an intermolecular ion pair <ref name="thompson" />.
+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 one α-helix and two antiparallel β-sheets <ref>[http://www.uniprot.org/uniprot/P02741 "UniProtKB"]</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 noticed for the residues 43 and 185 <ref name="kumar"/>. The residues Glu197 and Lys123 of CRP form an intermolecular ion pair <ref name="thompson" />.
 The diameter of the CRP pentamer is 102 Å, the inner pore diameter is 30 Å and the diameter of a subunit is 36 Å <ref name="agrawal">A. Agrawal, P. P. Singh, B. Bottazzi, C. Garlanda, A. Mantovani, Pattern recognition by Pentraxins, Adv Exp Med Biol. 2009; 653: 98-116</ref>.
 === Ca<sup>2+</sup> binding-site ===