Sandbox207: Difference between revisions
Elise Rosati (talk | contribs) No edit summary |
Elise Rosati (talk | contribs) No edit summary |
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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. | ||
{{STRUCTURE_1gnh| PDB=1gnh | SCENE= }} | |||
CRP -- C-reactive protein | CRP -- C-reactive protein | ||
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[[Image:Image2.jpg|300px|right|thumb| CRP structure]] | [[Image:Image2.jpg|300px|right|thumb| CRP structure]] | ||
==Structure== | ==Structure== | ||
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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 | 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. | ||