Sandbox207: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Elise Rosati (talk | contribs) No edit summary |
Elise Rosati (talk | contribs) No edit summary |
||
| Line 29: | Line 29: | ||
: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. [http://biology.kenyon.edu/BMB/Chime2/2005/Jenny/FRAMES/] | :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. [http://biology.kenyon.edu/BMB/Chime2/2005/Jenny/FRAMES/] | ||
[[Image:Image1.jpg| | [[Image:Image1.jpg|500px|right|thumb| '''Molecular structure and morphology of human CRP.''' | ||
(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]]] | |||