Sandbox207: Difference between revisions

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==CRP, C-reactive Protein==

The C Reactive Protein is a protein of the '''acute phase''', the first described, exclusively synthetized by the liver.

::The C Reactive Protein is a protein of the '''acute phase''', the first described, exclusively synthetized by the liver.

The CRP was first isolated by '''Tillett and France in 1930''', in patients' serum presenting an acute inflammation. This protein reacted to the '''polysaccharide C''' of the pneumocoque, that is where its name comes from. [http://www.rndsystems.com/cb_detail_objectname_SU05_CReactiveProtein.aspx <1>]

The CRP contributes to innate host defense, and plays an important role in inflammatory reactions. It can bind to specific molecular configurations typically exposed during cell death or found on the surfaces of pathogens. It is used as '''biological marker''' to reveal an inflammatory reaction and tissue damage. [http://biology.kenyon.edu/BMB/Chime2/2005/Jenny/FRAMES/ <2>]

:The CRP contributes to innate host defense, and plays an important role in inflammatory reactions. It can bind to specific molecular configurations typically exposed during cell death or found on the surfaces of pathogens. It is used as '''biological marker''' to reveal an inflammatory reaction and tissue damage. [http://biology.kenyon.edu/BMB/Chime2/2005/Jenny/FRAMES/ <2>]

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===Detailed strucutre===

:Each ~~promoter~~ consists of two anti-parallel β sheets (the lectin fold) with an α helix on the effector face of the protein. The ligand biding site is located on the concave face of the protein, and is composed of loops with 2 calcium ions bound 4 Å apart by protein side-chains.

:Each protomer consists of two '''anti-parallel β sheets''' (the lectin fold) with an '''α helix''' on the effector face of the protein. The ligand biding site is located on the concave face of the protein, and is composed of loops with 2 calcium ions bound 4 Å apart by protein side-chains.

:The recognition face contains the which consists of two coordinated calcium ions next to a hydrophobic pocket in which the phosphocholine stays.

:There are interpromoter interactions between the subunits: three salt bridges are included and the 115-123 loop of one protomer and the 40-42 and 197-202 regions of adjacent protomers are involved. Moreover, the subunits are capable to rotate by 15-20° around an axis parallel to the central alpha-helix.

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@@ Line 10: / Line 10: @@
 ==CRP, C-reactive Protein==
-The C Reactive Protein is a protein of the '''acute phase''', the first described, exclusively synthetized by the liver.
+::The C Reactive Protein is a protein of the '''acute phase''', the first described, exclusively synthetized by the liver.
 The CRP was first isolated by '''Tillett and France in 1930''', in patients' serum presenting an acute inflammation. This protein reacted to the '''polysaccharide C''' of the pneumocoque, that is where its name comes from. [http://www.rndsystems.com/cb_detail_objectname_SU05_CReactiveProtein.aspx <1>]
-The CRP contributes to innate host defense, and plays an important role in inflammatory reactions. It can bind to specific molecular configurations typically exposed during cell death or found on the surfaces of pathogens. It is used as '''biological marker''' to reveal an inflammatory reaction and tissue damage. [http://biology.kenyon.edu/BMB/Chime2/2005/Jenny/FRAMES/ <2>]
+:The CRP contributes to innate host defense, and plays an important role in inflammatory reactions. It can bind to specific molecular configurations typically exposed during cell death or found on the surfaces of pathogens. It is used as '''biological marker''' to reveal an inflammatory reaction and tissue damage. [http://biology.kenyon.edu/BMB/Chime2/2005/Jenny/FRAMES/ <2>]
@@ Line 31: / Line 31: @@
 ===Detailed strucutre===
-:Each promoter consists of two anti-parallel β sheets (the lectin fold) with an α helix on the effector face of the protein. The ligand biding site is located on the concave face of the protein, and is composed of loops with 2 calcium ions bound 4 Å apart by protein side-chains.
+:Each protomer consists of two '''anti-parallel β sheets''' (the lectin fold) with an '''α helix''' on the effector face of the protein. The ligand biding site is located on the concave face of the protein, and is composed of loops with 2 calcium ions bound 4 Å apart by protein side-chains.
 :The recognition face contains the which consists of two coordinated calcium ions next to a hydrophobic pocket in which the phosphocholine stays.
 :There are interpromoter interactions between the subunits: three salt bridges are included and the 115-123 loop of one protomer and the 40-42 and 197-202 regions of adjacent protomers are involved. Moreover, the subunits are capable to rotate by 15-20° around an axis parallel to the central alpha-helix.