Human Prion Protein Dimer: Difference between revisions
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<StructureSection load='1qlx' size='450' side='right' caption='' scene=''> | <StructureSection load='1qlx' size='450' side='right' caption='Human prion protein (PDB code [[1qlx]])' scene=''> | ||
== Prions as a disease causing agent== | == Prions as a disease causing agent== | ||
[[Image:1i4m.png| | [[Image:1i4m.png|left|150px|thumb|Human Prion Protein in dimer form [[1i4m]]]] | ||
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[[Image:10131_lores.jpg|left|300px|thumb|Pictomicrograph of Creutzfeldt-Jakob positive brain tissue|Caption: Holes in this sponge like brain tissue result from pockets of prion aggregation <ref>[http://phil.cdc.gov/PHIL_Images/10131/10131_lores.jpg Image of Creutzfeldt-Jakob positive brain tissue] was obtained from The CDC's Public Health Image Library.</ref>]] | |||
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[http://en.wikipedia.org/wiki/Prion Prions] are infectious or genetically coded misfolded proteins which act as templates upon which properly folded prion protein monomers can aggregate. Prions contain no nucleic acid such as other infectoius molecules or organisms. Human Prion Protein or Major Prion protein, exists as a normal constituent of human cells, found mostly in the brain<ref>Centers for Disease Control and Prevention: Prions. http://www.cdc.gov/ncidod/dvrd/prions/</ref> and is called PrP<sup>C</sup>.<ref name="Prusiner">PMID:9811807</ref> PrP<sup>C</sup> is composed of mostly helix whereas the infectious form, PrP<sup>Sc</sup> (also known as "scrapie" form), is composed of high percentage beta sheets.<ref name="Prusiner">PMID:9811807</ref> | [http://en.wikipedia.org/wiki/Prion Prions] are infectious or genetically coded misfolded proteins which act as templates upon which properly folded prion protein monomers can aggregate. Prions contain no nucleic acid such as other infectoius molecules or organisms. Human Prion Protein or Major Prion protein, exists as a normal constituent of human cells, found mostly in the brain<ref>Centers for Disease Control and Prevention: Prions. http://www.cdc.gov/ncidod/dvrd/prions/</ref> and is called PrP<sup>C</sup>.<ref name="Prusiner">PMID:9811807</ref> PrP<sup>C</sup> is composed of mostly helix whereas the infectious form, PrP<sup>Sc</sup> (also known as "scrapie" form), is composed of high percentage beta sheets.<ref name="Prusiner">PMID:9811807</ref> | ||
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[[Image:F4.large.jpg| | [[Image:F4.large.jpg|left|300px|thumb|Electrostatic potential alteration E200K|Caption: This shows (a&c) the electrostatic potential of wild-type Human Prion Protein with Glu200 and (b&d) the electrostatic potential of variant Lys200. <ref name="Zhang">PMID:10954699</ref>]] | ||
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=== PrP<sup>Sc</sup> === | === PrP<sup>Sc</sup> === | ||
The majority of this structure is <scene name='User:Erin_May/Sandbox_1/Beta_sheets/1'>beta sheets</scene>. | The majority of this structure is <scene name='User:Erin_May/Sandbox_1/Beta_sheets/1'>beta sheets</scene>. | ||
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The Cystine residues which were formerly part of disulfide bonds have been reduced catalytically without any chemical reducing agent. <ref name="Knaus">PMID:11524679</ref> | The Cystine residues which were formerly part of disulfide bonds have been reduced catalytically without any chemical reducing agent. <ref name="Knaus">PMID:11524679</ref> | ||
===Dimer Form=== | ===Dimer Form=== | ||
< | <scene name='Human_Prion_Protein_Dimer/Cv/1'>Major Prion Protein: Dimerized</scene> [[1i4m]]. | ||
The <scene name='User:Erin_May/Sandbox_1/Previously_shown_residues/1'>residues</scene>, shown above, alter the function of Major Prion Protein's ability to re-fold, however their positions on the wild-type monomer and fully unfolded PrP<sup>Sc</sup>, do not illustrate a clear mechanism for propagation. The dimer brings light to these residues' influence on the infectious qualities of PrP<sup>Sc</sup>. | The <scene name='User:Erin_May/Sandbox_1/Previously_shown_residues/1'>residues</scene>, shown above, alter the function of Major Prion Protein's ability to re-fold, however their positions on the wild-type monomer and fully unfolded PrP<sup>Sc</sup>, do not illustrate a clear mechanism for propagation. The dimer brings light to these residues' influence on the infectious qualities of PrP<sup>Sc</sup>. | ||