Sandbox Reserved 1121

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 5: Line 5:
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
-
The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<ref name="kumar"/>
+
The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.<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>
== Structure ==
== Structure ==
Line 12: Line 12:
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" />
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>
+
CRP is a calcium dependent strcuture. Effectively, Ca2+ is required for PC binding, and more precisely for the formation of the PCbinding site. Structural rearrangements of the CRP occur when the protein binds calcium. The protection against denaturation and proteolysis. <ref name="ramadan">Ramadan, M. A. M., Shrive, A. K., Holden, D., Myles, D. A. A., Volanakis, J. E., Larry J.DeLucas, L. J., Greenhough, T. J. (2002), The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals, Acta Cryst., D58 :992-1001</ref>
 +
 
=== PC binding site ===
=== PC binding site ===
PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/>
PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.<ref name="thompson">Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.</ref> Phe-66 and Glu-81 are the two key residues that enable the binding of PC. <ref name="kumar"/>

Revision as of 20:50, 26 January 2016

This Sandbox is Reserved from 15/12/2015, through 15/06/2016 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1120 through Sandbox Reserved 1159.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Human C-reactive protein complexed with phosphocholine

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 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
  4. ↑ http://www.uniprot.org/uniprot/P02741
  5. ↑ http://www.unco.edu/nhs/Chemistry/faculty/dong/pub/pentraxin.pdf
  6. ↑ 6.0 6.1 6.2 Thompson, D., Pepys, M. B., Wood, S. P. (1999), The physiological structure of human C-reactive protein and its complex with phosphocholine, Structure February 1999, 7:169–177.
  7. ↑ Ramadan, M. A. M., Shrive, A. K., Holden, D., Myles, D. A. A., Volanakis, J. E., Larry J.DeLucas, L. J., Greenhough, T. J. (2002), The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals, Acta Cryst., D58 :992-1001
Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_1121"
Personal tools