Sandbox Reserved 821: Difference between revisions

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== '''Structure of CRP''' ==

~~<Structure load='1gnh' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />~~

CRP is a pentamer: it contains five identical 23-kDa protomers, noncovalently associated (van der Waals contacts or hydrogen bonding) around a central pore. All members of the “pentraxins” family have this general structure.

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==='''''Calcium'''''===

There are two <scene name='56/568019/Structure_of_crp_v2/1'>calcium-binding sites</scene> per CRP protomer.

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Phosphocholine is an universal phospholipid found particularly in the cell membranes and plasma lipoproteins of bacteria, fungi, plants and other eukaryotic organisms whose us, the human beings. However, CRP can only bind phosphocholine of our damaged or apoptotic cells, as head groups of phosphocholine are inaccessible to CRP in “normal” cells.

~~Different sites of the CRP are needed to bind phosphocholine:~~

- A hydrophobic pocket with the two key residues Phe66 and Glu81 located on the two extremities of the cavity. Phe66 interacts with the methyl group of the phosphocholine by hydrophobic interactions. Glu81 interacts with the positively charged choline nitrogen of the phosphocholine. The existence of this hydrophobic pocket (lined by Glu81, Gly79, Asn61 and Thr76) would allow bindings of phosphocholine analogues, maybe with higher affinity. This property is very interesting for the research of new drugs blocking the effects of CRP, sometimes harmful.

~~- The two bound calcium ions which interact with the phosphate group of the phosphocholine (two oxygen of the phosphate group).~~

The role of CRP to protect the host of infection and inflammation is thus certainly done first by binding to phosphocholine or other ligands such as phosphoethanolamine, and then by activation of the classical complement pathway via interaction with C1q or phagocytosis via interaction with Fc receptors.

Phosphocholine is an universal phospholipid found particularly in the cell membranes and plasma lipoproteins of bacteria, fungi, plants and other eukaryotic organisms whose us, the human beings. However, CRP can only bind phosphocholine of our damaged or apoptotic cells, as head groups of phosphocholine are inaccessible to CRP in “normal” cells.

Different sites of the CRP are needed to bind phosphocholine:

- A hydrophobic pocket with the two key residues Phe66 and Glu81 located on the two extremities of the cavity. Phe66 interacts with the methyl group of the phosphocholine by hydrophobic interactions. Glu81 interacts with the positively charged choline nitrogen of the phosphocholine. The existence of this hydrophobic pocket (lined by Glu81, Gly79, Asn61 and Thr76) would allow bindings of phosphocholine analogues, maybe with higher affinity. This property is very interesting for the research of new drugs blocking the effects of CRP, sometimes harmful.

- The two bound calcium ions which interact with the phosphate group of the phosphocholine (two oxygen of the phosphate group).

The role of CRP to protect the host of infection and inflammation is thus certainly done first by binding to phosphocholine or other ligands such as phosphoethanolamine, and then by activation of the classical complement pathway via interaction with C1q or phagocytosis via interaction with Fc receptors.

Sandbox Reserved 821: Difference between revisions

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@@ Line 16: / Line 16: @@
 == '''Structure of CRP''' ==
-<Structure load='1gnh' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
 CRP is a pentamer: it contains five identical 23-kDa protomers, noncovalently associated (van der Waals contacts or hydrogen bonding) around a central pore. All members of the “pentraxins” family have this general structure.
@@ Line 26: / Line 25: @@
 ==='''''Calcium'''''===
+<Structure load='1gnh' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
 There are two <scene name='56/568019/Structure_of_crp_v2/1'>calcium-binding sites</scene> per CRP protomer.
@@ Line 54: / Line 54: @@
-Phosphocholine is an universal phospholipid found particularly in the cell membranes and plasma lipoproteins of bacteria, fungi, plants and other eukaryotic organisms whose us, the human beings. However, CRP can only bind phosphocholine of our damaged or apoptotic cells, as head groups of phosphocholine are inaccessible to CRP in “normal” cells.
-Different sites of the CRP are needed to bind phosphocholine:
-- A hydrophobic pocket with the two key residues Phe66 and Glu81 located on the two extremities of the cavity. Phe66 interacts with the methyl group of the phosphocholine by hydrophobic interactions. Glu81 interacts with the positively charged choline nitrogen of the phosphocholine. The existence of this hydrophobic pocket (lined by Glu81, Gly79, Asn61 and Thr76) would allow bindings of phosphocholine analogues, maybe with higher affinity. This property is very interesting for the research of new drugs blocking the effects of CRP, sometimes harmful.
-- The two bound calcium ions which interact with the phosphate group of the phosphocholine (two oxygen of the phosphate group).
-The role of CRP to protect the host of infection and inflammation is thus certainly done first by binding to phosphocholine or other ligands such as phosphoethanolamine, and then by activation of the classical complement pathway via interaction with C1q or phagocytosis via interaction with Fc receptors.
+Phosphocholine is an universal phospholipid found particularly in the cell membranes and plasma lipoproteins of bacteria, fungi, plants and other eukaryotic organisms whose us, the human beings. However, CRP can only bind phosphocholine of our damaged or apoptotic cells, as head groups of phosphocholine are inaccessible to CRP in “normal” cells.
+Different sites of the CRP are needed to bind phosphocholine:
+- A hydrophobic pocket with the two key residues Phe66 and Glu81 located on the two extremities of the cavity. Phe66 interacts with the methyl group of the phosphocholine by hydrophobic interactions. Glu81 interacts with the positively charged choline nitrogen of the phosphocholine. The existence of this hydrophobic pocket (lined by Glu81, Gly79, Asn61 and Thr76) would allow bindings of phosphocholine analogues, maybe with higher affinity. This property is very interesting for the research of new drugs blocking the effects of CRP, sometimes harmful.
+- The two bound calcium ions which interact with the phosphate group of the phosphocholine (two oxygen of the phosphate group).
+The role of CRP to protect the host of infection and inflammation is thus certainly done first by binding to phosphocholine or other ligands such as phosphoethanolamine, and then by activation of the classical complement pathway via interaction with C1q or phagocytosis via interaction with Fc receptors.