Sandbox Reserved 474

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== Structure and Function ==
== Structure and Function ==
CRPs 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.
CRPs 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.
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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

Revision as of 19:22, 30 April 2012

==Your Heading Here (maybe something like 'Structure')==

Structure of Human C-Reactive Protein (PDB entry 1gnh)

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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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Structure and Function

CRPs 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

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