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== | ||
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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>]] | ||
{{clear}} | |||
=== 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>. | ||