Sandbox Reserved 1121: Difference between revisions

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PC stands for phosphocholine. It is a phospholipid in cell membranes and a plasma lipoproteins <ref name="thompson"/>. Phe-66 and Glu-81 are the two key residues that enable the binding of PC <ref name="kumar"/>. They interact with the choline function of PC, which therefore lies inside the PC-binding site.

CRP binds the phosphocholine and other ligands in a Ca2+-dependent way. The PC-binding site is next to the Ca2+-binding sites on the same face of the CRP protein. The PC-binding site is a hydrophobic pocket constituted by the residues Leu64, Phe66, Thr76 and the two Ca2+. The phosphate groupe of PC interacts by coordination with the two Ca2+.

The affinity of CRP for PC increases with the concentration of PC. A surface containing a high density of PC, such as C-polycaccharide, is therefore propitious ~~for~~ the CRP-binding <ref name="duclos"/>.

The affinity of CRP for PC increases with the concentration of PC. A surface containing a high density of PC, such as C-polycaccharide, is therefore propitious to the CRP-binding <ref name="duclos"/>.

CRP can also bind chromatin, histones, small nuclear robonucleoproteins nuclear envelop proteins and nucleosomes Ca2+-dependently <ref name="agrawal"/>.

[[Image:Phosphocholine.PNG | thumb | ~~Phosphocholine~~ and Ca2+-binding site <ref>The PyMOL Molecular Graphics System, Version 1.8 Schrödinger, LLC.</ref>]]

[[Image:Phosphocholine.PNG | thumb | PC and Ca2+-binding site <ref>The PyMOL Molecular Graphics System, Version 1.8 Schrödinger, LLC.</ref>]]

== Function ==

Sandbox Reserved 1121: Difference between revisions

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 PC stands for phosphocholine. It is a phospholipid in cell membranes and a plasma lipoproteins <ref name="thompson"/>. Phe-66 and Glu-81 are the two key residues that enable the binding of PC <ref name="kumar"/>. They interact with the choline function of PC, which therefore lies inside the PC-binding site.
 CRP binds the phosphocholine and other ligands in a Ca<sup>2+</sup>-dependent way. The PC-binding site is next to the Ca<sup>2+</sup>-binding sites on the same face of the CRP protein. The PC-binding site is a hydrophobic pocket constituted by the residues Leu64, Phe66, Thr76 and the two Ca<sup>2+</sup>. The phosphate groupe of PC interacts by coordination with the two Ca<sup>2+</sup>.
-The affinity of CRP for PC increases with the concentration of PC. A surface containing  a high density of PC, such as C-polycaccharide, is therefore propitious for the CRP-binding <ref name="duclos"/>.
+The affinity of CRP for PC increases with the concentration of PC. A surface containing  a high density of PC, such as C-polycaccharide, is therefore propitious to the CRP-binding <ref name="duclos"/>.
 CRP can also bind chromatin, histones, small nuclear robonucleoproteins nuclear envelop proteins and nucleosomes Ca<sup>2+</sup>-dependently <ref name="agrawal"/>.
-[[Image:Phosphocholine.PNG | thumb | Phosphocholine and Ca<sup>2+</sup>-binding site <ref>The PyMOL Molecular Graphics System, Version 1.8 Schrödinger, LLC.</ref>]]
+[[Image:Phosphocholine.PNG | thumb | PC and Ca<sup>2+</sup>-binding site <ref>The PyMOL Molecular Graphics System, Version 1.8 Schrödinger, LLC.</ref>]]
 == Function ==