Sandbox Reserved 1121: Difference between revisions

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

=== Ca2+ binding-site ===

CRP is a calcium dependent structure. Effectively, Ca2+ is required for PC binding, and more precisely for the formation of the PC binding site thanks to structural rearrangements. The protection against denaturation and proteolysis is performed through Ca2+ binding too. In the absence of Ca2+, hCRP is cleaved between Asn145 and Phe146 by nagarse protease, and between Phe146 and Glu147 by pronase.

Sandbox Reserved 1121: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ 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 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 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 four α-helices and three antiparallel 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 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 diameterof the CRP pentamer is 102 Å, the inner pore diameter is 30 Å and the diameter of a subunit is 36 Å. <ref>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 ===
 CRP is a calcium dependent structure. Effectively, Ca<sup>2+</sup> is required for PC binding, and more precisely for the formation of the PC binding site thanks to structural rearrangements. The protection against denaturation and proteolysis is performed through Ca<sup>2+</sup> binding too. In the absence of Ca<sup>2+</sup>, hCRP is cleaved between Asn145 and Phe146 by nagarse protease, and between Phe146 and Glu147 by pronase.