Human Prion Protein Dimer: Difference between revisions
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The following interactions and residue switching portray possible catalytic sites: | The following interactions and residue switching portray possible catalytic sites: | ||
Residues 129, 200, and 164 to 170 are shown to exist right at the dimer interfaces | Residues 129, 200, and 164 to 170 are shown to exist right at the dimer interfaces. The location of these residues within the dimer indicates that their key operation is found somewhere in the dimerization process. <ref name="Lee">PMID:19927125</ref><ref name="Knaus">PMID:11524679</ref><ref name="Zhang">PMID:10954699</ref> | ||
Helix 1 (Ser 143−Tyr 157) exists at the <scene name='User:Erin_May/Sandbox_1/Nonpolar_at_dimer_interface/2'>dimer interface</scene>. Many nonpolar residues form Van der Waals attractions. Acidic and mostly negative residues are shown in blue. Basic and mostly positive residues are shown in red. The interactions between these also stabilize the dimer interface. | Helix 1 (Ser 143−Tyr 157) exists at the <scene name='User:Erin_May/Sandbox_1/Nonpolar_at_dimer_interface/2'>dimer interface</scene>. Many nonpolar residues form Van der Waals attractions. Acidic and mostly negative residues are shown in blue. Basic and mostly positive residues are shown in red. The interactions between these also stabilize the dimer interface. | ||