Sandbox Reserved 1121: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Lucile Guyot (talk | contribs) No edit summary |
Lucile Guyot (talk | contribs) No edit summary |
||
| Line 1: | Line 1: | ||
<Structure load='1B09' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_ESBS_2015}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | <Structure load='1B09' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />{{Sandbox_Reserved_ESBS_2015}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
== Human C-reactive protein complexed with phosphocholine == | == Human C-reactive protein complexed with phosphocholine == | ||
Human C-Reactive Protein (CRP) is an acute phase protein belonging to the highly conserved pentraxin protein family <ref name="Thompson">PMID: 10368284</ref>. Althought it is a normal serum protein, its circulating concentration raises rapidly and extensively in a cytokine-mediated in response to infection, an inflammation or a tissue injury | |||
<ref name="Thompson"/>. | |||
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| Line 10: | Line 13: | ||
=== 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 | The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 kDa protein consisting of 224 residues bound together. The secondary structure is formed of one <scene name='71/719862/Helix/1'>α-helix</scene> and two antiparallel <scene name='71/719862/Sheet/1'>β-sheets</scene> <ref>[http://www.uniprot.org/uniprot/P02741 UniProtKB - P02741 (CRP_HUMAN)]</ref>. The predominant structure is β-sheet <ref>PMID: 1382589</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">PMID: 10368284</ref>. | ||
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">PMID: 19799114 </ref>. | 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">PMID: 19799114 </ref>. | ||
| Line 37: | Line 40: | ||
== References == | == References == | ||
<references/> | <references/> | ||
