Sandbox207: Difference between revisions

Line 39:

(a) Negatively stained electron micrograph showing the typical pentameric disc-like structure face-on and side-on (arrows). (b) Ribbon diagram of the crystal structure, showing the lectin fold and the two calcium atoms (spheres) in the ligand-binding site of each protomer. (c) Space-filling model of the CRP molecule, showing a single phosphocholine molecule located in the ligand-binding site of each protomer.[http://www.jci.org/articles/view/18921 <3>]]]

: Thanks to this rotation, the alpha-helices can lie closer to the axis of the pentamere, therefore bringing the bound Ca2+ further away from it. On each subunit, we can find phosphocholine bound in a shallow surface pocket. With the help of phosphate groups and Glu81 via the choline moiety, the phosphocholine can interact with the two protein-bound ions.

: Thanks to this rotation, the alpha-helices can lie closer to the axis of the pentamere, therefore bringing the bound Ca2+ further away from it. On each subunit, we can find '''phosphocholine''' bound in a shallow surface pocket. With the help of phosphate groups and Glu81 via the choline moiety (??), the phosphocholine can '''interact''' with the two protein-bound ions.

:Moreover, the structure of CRP is different in ~~diseased~~ patients. Indeed, in some pathological conditions, the Human CRP is glycosylated. Analysis of the structure showed the systematic absence of two peptide fragments, one at the N-terminus (loop 1-6) in all patients, the other near the C-terminus (loop 189-191) in patients with osteogenic sarcoma and Cushing's syndrome. In ~~an undiseased~~ individual, glycosylation sites are inacessible due to the presence of the N-terminal. The loss of these two fragments exposed two potential glycosylation sites on a cleft door. The functional areas of the pentraxin structure ~~remains~~ the same since the Ca2+ and phosphocholine sites are on the opposite site of the pentraxin molecule. [http://biology.kenyon.edu/BMB/Chime2/2005/Jenny/FRAMES/ <2>]

:Moreover, the structure of CRP is different in ill patients. Indeed, '''in some pathological conditions''', the Human CRP is '''glycosylated'''. Analysis of the structure showed the systematic '''absence of two peptide fragments''', one at the N-terminus (loop 1-6) in all patients, the other near the C-terminus (loop 189-191) in patients with '''osteogenic sarcoma and Cushing's syndrome'''. In a healthy individual, '''glycosylation sites are inacessible due to the presence of the N-terminal'''. The loss of these two fragments exposed two potential glycosylation sites on a cleft door. The functional areas of the pentraxin structure remain the same since the Ca2+ and phosphocholine sites are on the opposite site of the pentraxin molecule. [http://biology.kenyon.edu/BMB/Chime2/2005/Jenny/FRAMES/ <2>]

Sandbox207: Difference between revisions

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@@ Line 39: / Line 39: @@
 (a) Negatively stained electron micrograph showing the typical pentameric disc-like structure face-on and side-on (arrows). (b) Ribbon diagram of the crystal structure, showing the lectin fold and the two calcium atoms (spheres) in the ligand-binding site of each protomer. (c) Space-filling model of the CRP molecule, showing a single phosphocholine molecule located in the ligand-binding site of each protomer.[http://www.jci.org/articles/view/18921 <3>]]]
-: Thanks to this rotation, the alpha-helices can lie closer to the axis of the pentamere, therefore bringing the bound Ca2+ further away from it. On each subunit, we can find phosphocholine bound in a shallow surface pocket. With the help of phosphate groups and Glu81 via the choline moiety, the phosphocholine can interact with the two protein-bound ions.
+: Thanks to this rotation, the alpha-helices can lie closer to the axis of the pentamere, therefore bringing the bound Ca2+ further away from it. On each subunit, we can find '''phosphocholine''' bound in a shallow surface pocket. With the help of phosphate groups and Glu81 via the choline moiety (??), the phosphocholine can '''interact''' with the two protein-bound ions.
-:Moreover, the structure of CRP is different in diseased patients. Indeed, in some pathological conditions, the Human CRP is glycosylated. Analysis of the structure showed the systematic absence of two peptide fragments, one at the N-terminus (loop 1-6) in all patients, the other near the C-terminus (loop 189-191) in patients with osteogenic sarcoma and Cushing's syndrome. In an undiseased individual, glycosylation sites are inacessible due to the presence of the N-terminal. The loss of these two fragments exposed two potential glycosylation sites on a cleft door. The functional areas of the pentraxin structure remains the same since the Ca2+ and phosphocholine sites are on the opposite site of the pentraxin molecule. [http://biology.kenyon.edu/BMB/Chime2/2005/Jenny/FRAMES/ <2>]
+:Moreover, the structure of CRP is different in ill patients. Indeed, '''in some pathological conditions''', the Human CRP is '''glycosylated'''. Analysis of the structure showed the systematic '''absence of two peptide fragments''', one at the N-terminus (loop 1-6) in all patients, the other near the C-terminus (loop 189-191) in patients with '''osteogenic sarcoma and Cushing's syndrome'''. In a healthy individual, '''glycosylation sites are inacessible due to the presence of the N-terminal'''. The loss of these two fragments exposed two potential glycosylation sites on a cleft door. The functional areas of the pentraxin structure remain the same since the Ca2+ and phosphocholine sites are on the opposite site of the pentraxin molecule. [http://biology.kenyon.edu/BMB/Chime2/2005/Jenny/FRAMES/ <2>]