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This page is reserveted for a work from two students in ESBS (A.Butet and E.Rosati) | This page is reserveted for a work from two students in ESBS (A.Butet and E.Rosati) | ||
Thanks. | Thanks. | ||
CRP -- C-reactive protein | |||
Structure : | |||
- Gene : exon, intron ? | |||
- Taille de la protéine | |||
- Sécrétion | |||
- Structure détaillée | |||
- Famille | |||
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. 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. | |||
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. | |||
It exists 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 and 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. | |||
The pentraxin family is highly conserved in evolution. | |||