Sandbox207
From Proteopedia
(Difference between revisions)
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: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 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=== | ===Size=== | ||
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===Detailed strucutre=== | ===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 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. |
Revision as of 14:55, 26 December 2011
This page is reserveted for a work from two students in ESBS (A.Butet and E.Rosati) Thanks.
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| 1gnh, resolution 3.00Å () | |||||||||
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| Ligands: | |||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
[b] C-reactive protein, CRP [/b]
Image:Image2.jpg
CRP structure
Contents |
Structure
- Gene : exon, intron ? - Taille de la protéine - Sécrétion - Structure détaillée - Famille
Exon, intron, family
- 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.
Size
- Each subunit contains 206 amino acid residues (approximately 23kDa) and is non-glycosylated. The outside diameter of the pentamer is 102 Å, the diameter of the inner core is 30 Å, and the diameter of the protomer is 36 Å.
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.
- 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.
