MillerSandbox1
Miller_Sandbox1
This is a default text for your page MillerSandbox1. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. BackgroundThroughout the medical field, the Human C-Reactive Protein (CRP) has been used to clinically determine whether or not there is an infection, tissue injury, or an inflammatory response occurring within the body. Thus, CRP is a major acute-phase protein, in which its concentration can reach levels upwards of 1000+mg/L (Pathak and Agrawal 6). In comparison, normal CRP levels within the human body are referenced to be estimated at 0.8mg/L depending on the subject. In a pathophysiological sense, CRP has been researched to be a "significant predictor of future cardiac episodes" (Boncler et al.). With that, CRP is determined to play a specific role in both physiological and pathophysiological aspects within the human body. StructureCRP has a mass of 23kDa per subunit with 206 amino acid residues because it is a pentameric protein, which means it is "composed of five identical noncovalently bound subunits" (Pathak and Agrawal 6). Functionally, CRP will "bind to [phosphocholine] PCh in a Ca - dependent manner" (Pathak and Agrawal 6); moreover, CRP has five binding sites for PCh, one on each subunit (Pathak and Agrawal 6). Some of the amino acids that are directly present in the binding sites include, Glu81, Phe66, and Thr76. The Glu81 forms hydrogen bonds with the nitrogen atom that is within the choline group of the PCh, "Phe66 interacts with three methyl groups of choline" (Pathak and Agrawal 6), and the Thr76 is a crucial aspect in opening the binding site to an appropriate size for the PCh (Pathak and Agrawal 6). Furthermore, PCh's phosphate group is interactive with two Ca2+ molecules that are bound to the CRP (Pathak and Agrawal 6). The Ca2+ is the bound ligand to the C-reactive protein with two calcium ions per protomer. DiseaseRelevanceStructural highlightsThis is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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