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== Structure of CRP promoter ==
== Structure of CRP promoter ==
Based on homology modeling, CRP structure was found to be similar to that of SAP. The subunits within the structure consisted of a two-layered β sheet with a flattened jelly roll topology. Additionally, there is a presence of two calcium ions that are bound 4 Å apart by protein sidechains, and this is the site of ligand binding, which is referred to as the B side. The other side, designated A hosts a single α, and the pentameric disc shows five helices on one side with ten calcuim ions on the other. The side walls on the A face are constructed from Ser5, Arg6, Gln203, Pro206, Trp187, Arg188, Asn160, Gly177, Leu176, Try175, His95 and Asp112. The bottom side of CRP consiss of ASn158, His38, Leu37, Val94 and Asp112.
Based on homology modeling, CRP structure was found to be similar to that of SAP. The subunits within the structure consisted of a two-layered β sheet with a flattened jelly roll topology. Additionally, there is a presence of two calcium ions that are bound 4 Å apart by protein sidechains, and this is the site of ligand binding, which is referred to as the B side. The other side, designated A hosts a single α, and the pentameric disc shows five helices on one side with ten calcuim ions on the other. The side walls on the A face are constructed from Ser5, Arg6, Gln203, Pro206, Trp187, Arg188, Asn160, Gly177, Leu176, Try175, His95 and Asp112. The bottom side of CRP consiss of ASn158, His38, Leu37, Val94 and Asp112.
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== Biological Implications ==
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It is known that CRP belongs to a highly conserved pentraxin class that is responsible for innate immunity and it aids in the prevention of developing an autoimmunity [1] COmplexed or aggregated CRP activates complent, with pro-inflammatory effects. For instance, a direct correlation has been made between increased levels of CRP to complications of atherosslerosis which may include a mycardial infarction. In addition, CRP has the ability to predict future outcomes as a result of the infarction. Furthermore, it was discovered that CRP actually
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== Structure of CRP pentamer ==
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In CRP, each subunit in CRP is rotated by 22° towards the five-fold axis in comparison to SAP, where the subunits are planar to each other.Also,
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== Comparison of human CRP to other pentraxins ==
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When the CRP structure is complexed with PC, major interactions that occur between two phosphate oxygens and the calciums and between the positively charged quaternary nitrogen of PC and the negatively charged sidechain of Glu81. Also, another difference is the ability f
== CRP Role in Atherosclerosis ==
== CRP Role in Atherosclerosis ==
Human 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
Human 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

Revision as of 18:50, 2 May 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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Contents

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

Structure of CRP promoter

Based on homology modeling, CRP structure was found to be similar to that of SAP. The subunits within the structure consisted of a two-layered β sheet with a flattened jelly roll topology. Additionally, there is a presence of two calcium ions that are bound 4 Å apart by protein sidechains, and this is the site of ligand binding, which is referred to as the B side. The other side, designated A hosts a single α, and the pentameric disc shows five helices on one side with ten calcuim ions on the other. The side walls on the A face are constructed from Ser5, Arg6, Gln203, Pro206, Trp187, Arg188, Asn160, Gly177, Leu176, Try175, His95 and Asp112. The bottom side of CRP consiss of ASn158, His38, Leu37, Val94 and Asp112.

Biological Implications

It is known that CRP belongs to a highly conserved pentraxin class that is responsible for innate immunity and it aids in the prevention of developing an autoimmunity [1] COmplexed or aggregated CRP activates complent, with pro-inflammatory effects. For instance, a direct correlation has been made between increased levels of CRP to complications of atherosslerosis which may include a mycardial infarction. In addition, CRP has the ability to predict future outcomes as a result of the infarction. Furthermore, it was discovered that CRP actually

Structure of CRP pentamer

In CRP, each subunit in CRP is rotated by 22° towards the five-fold axis in comparison to SAP, where the subunits are planar to each other.Also,

Comparison of human CRP to other pentraxins

When the CRP structure is complexed with PC, major interactions that occur between two phosphate oxygens and the calciums and between the positively charged quaternary nitrogen of PC and the negatively charged sidechain of Glu81. Also, another difference is the ability f

CRP Role in Atherosclerosis

Human 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

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