Sandbox Reserved 1121

From Proteopedia

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== Structure ==
== Structure ==
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=== Primary structure ===
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=== CRP structure ===
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Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequenceof CRP.<ref name="kumar"/>
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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"/>
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===Secondary structure and more===
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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> 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> Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.<ref name="thompson" />
=== Calcium binding-site ===
=== Calcium binding-site ===

Revision as of 20:16, 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.
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Human C-reactive protein complexed with phosphocholine

Caption for this structure

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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 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.
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