Sandbox207: Difference between revisions

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==Structure==
==Structure==
[[Image:Struc2.jpg|300px|right|thumb| CRP structure [http://news.sciencemag.org/sciencenow/2009/06/30-02.html <7>]]]
[[Image:Struc2.jpg|300px|right|thumb| CRP structure [http://news.sciencemag.org/sciencenow/2009/06/30-02.html <6>]]]


===Gene structure, family===
===Gene structure, family===
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:After this connection, CRP activates the '''classical complement pathway''' in the absence of antibody, and '''opsonizes ligands''', with the aim of their phagocytosis.
:After this connection, CRP activates the '''classical complement pathway''' in the absence of antibody, and '''opsonizes ligands''', with the aim of their phagocytosis.
:Indeed, when CRP is bound to the ligand, it is recognized by the factor '''CIq''', which activates powerfully the classical complement pathway, committing the factor C3. Then there is formation of the membrane attack complex C5-C9 on the surface of the ligand, what entails its phagocytosis.
:Indeed, when CRP is bound to the ligand, it is recognized by the factor '''CIq''', which activates powerfully the classical complement pathway, committing the factor C3. Then there is formation of the membrane attack complex C5-C9 on the surface of the ligand, what entails its phagocytosis.
:[http://www.ncbi.nlm.nih.gov/pubmed/11532280 <6>]
:[http://www.ncbi.nlm.nih.gov/pubmed/11532280 <5>]


:On the recognition face, there are two binding sites of equal affinity to calcium, consisting of residues <scene name='Sandbox207/Phosphocholine/4'>Asp60, Asn61, Glu138, Asp140, and the main chain carbonyl of Gln139 -in red-</scene> for the first calcium ion and residues<scene name='Sandbox207/Phosphocholine/5'>Glu138, Asp140, Gln150, and Glu147 -in green-</scene> for the second calcium ion. An interaction appears between the two calcium ions and the oxygens of the phosphate group and the choline group, which stays in a hydrophobic pocket formed by residues <scene name='Sandbox207/Phosphocholine/7'>Phe66, Leu64, Thr76, and Glu81</scene>. The face of Phe66 (in light blue) is exposed, allowing it to have '''hydrophobic interactions''' with the methyl groups of the choline. Glu81 (in magenta) interacts with the positively charged nitrogen on choline.
:On the recognition face, there are two binding sites of equal affinity to calcium, consisting of residues <scene name='Sandbox207/Phosphocholine/4'>Asp60, Asn61, Glu138, Asp140, and the main chain carbonyl of Gln139 -in red-</scene> for the first calcium ion and residues<scene name='Sandbox207/Phosphocholine/5'>Glu138, Asp140, Gln150, and Glu147 -in green-</scene> for the second calcium ion. An interaction appears between the two calcium ions and the oxygens of the phosphate group and the choline group, which stays in a hydrophobic pocket formed by residues <scene name='Sandbox207/Phosphocholine/7'>Phe66, Leu64, Thr76, and Glu81</scene>. The face of Phe66 (in light blue) is exposed, allowing it to have '''hydrophobic interactions''' with the methyl groups of the choline. Glu81 (in magenta) interacts with the positively charged nitrogen on choline.