Sandbox Reserved 474
From Proteopedia
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This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500. |
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More help: Help:Editing For more help, look at this link: http://www.proteopedia.org/wiki/index.php/Help:Getting_Started_in_Proteopedia Structure and FunctionCRPs five promoter structures are folded into two anti-parallel β-sheets with flattened jellyroll topologies. Each promoter contains a recognition face with a phosphocholine binding site consisting of two coordinated calcium ions adjacent to a hydrophobic pocket. The co-crystallized structure of CRP with phosphocholine suggest that Phe-66 and Glu-81 are two key residues that mediate binding between phosphocholine and CRP. More specifically, Phe-66 provides hydrophobic interactions with the methyl groups of phosphocholine. Similarly, Glu-81 is found on the opposite end of the pocket where it interacts well with the positively charged choline nitrogen. Present on the opposite face of the pentamer is the effector face, where the presumed C1q and Fcγ receptors bind
CRP Role in AtherosclerosisHuman Recombinant CRP has been determined to serve as a mediator of atherosclerosis. CRP has been shown to initiate IL-6 and endothelin-1 release from endothelial cells |