Sandbox207: Difference between revisions

Line 21:

:The CRP gene is located on chromosome 1q23. It is composed of two exons and one intron. This gene is regulated by interleukin-6, the principal inducer of the gene during the acute phase. CRP is secreted by hepatocytes.

The Human CRP belongs to the pentraxin family of proteins having five identical, non-covalently associated subunits that form a symmetrical homopentameric ring. The pentraxin family is highly conserved in evolution.

:The Human CRP belongs to the pentraxin family of proteins having five identical, non-covalently associated subunits that form a symmetrical homopentameric ring. The pentraxin family is highly conserved in evolution.

===Size===

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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.

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

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

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.

: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.

This rotation allows the alpha-helices to lie closer together to the pentameric 5-fold axis, and brings the bound Ca2+ further away from it. PC is bound in a shallow surface pocket on each subunit, interacting with the two protein-bound calcium ions by the phosphate group and with Glu81 via the choline moiety.

:This rotation allows the alpha-helices to lie closer together to the pentameric 5-fold axis, and brings the bound Ca2+ further away from it. PC is bound in a shallow surface pocket on each subunit, interacting with the two protein-bound calcium ions by the phosphate group and with Glu81 via the choline moiety.

Sandbox207: Difference between revisions

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@@ Line 21: / Line 21: @@
 :The CRP gene is located on chromosome 1q23. It is composed of two exons and one intron. This gene is regulated by interleukin-6, the principal inducer of the gene during the acute phase. CRP is secreted by hepatocytes.
-The Human CRP belongs to the pentraxin family of proteins having five identical, non-covalently associated subunits that form a symmetrical homopentameric ring. The pentraxin family is highly conserved in evolution.
+:The Human CRP belongs to the pentraxin family of proteins having five identical, non-covalently associated subunits that form a symmetrical homopentameric ring. The pentraxin family is highly conserved in evolution.
 ===Size===
@@ Line 29: / Line 29: @@
 ===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.
-The recognition face contains the which consists of two coordinated calcium ions next to a hydrophobic pocket in which the phosphocholine rests.
+:The recognition face contains the which consists of two coordinated calcium ions next to a hydrophobic pocket in which the phosphocholine rests.
-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.
+: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.
-This rotation allows the alpha-helices to lie closer together to the pentameric 5-fold axis, and brings the bound Ca2+ further away from it. PC is bound in a shallow surface pocket on each subunit, interacting with the two protein-bound calcium ions by the phosphate group and with Glu81 via the choline moiety.
+:This rotation allows the alpha-helices to lie closer together to the pentameric 5-fold axis, and brings the bound Ca2+ further away from it. PC is bound in a shallow surface pocket on each subunit, interacting with the two protein-bound calcium ions by the phosphate group and with Glu81 via the choline moiety.