Andrew Helmerich Sandbox 1: Difference between revisions
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<scene name='10/1038819/N_term_disulfide/1'>TextToBeDisplayed</scene> | <scene name='10/1038819/N_term_disulfide/1'>TextToBeDisplayed</scene> | ||
== Mechanism of Activation == | |||
===Two Domain Model of Amylin Binding=== | |||
== Disease == | == Disease == | ||
Revision as of 17:17, 4 April 2024
The Amylin Receptor(AMYR)The Amylin Receptor(AMYR)
IntroductionOverview and FunctionRole of AmylinAmylin history, role, etc Amylin Peptide Structure
StructureStructure Overview
Amidated C-Terminus
G-Alpha-TMD Interaction
N Terminus Dusulfide
Mechanism of ActivationTwo Domain Model of Amylin BindingDiseaseRelevanceStructural highlights
This is a sample scene created with SAT to by Group, and another to make 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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ReferencesReferences
- ↑ Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:http://dx.doi.org/10.1002/1873-3468.12677
- ↑ Cao J, Belousoff MJ, Liang YL, Johnson RM, Josephs TM, Fletcher MM, Christopoulos A, Hay DL, Danev R, Wootten D, Sexton PM. A structural basis for amylin receptor phenotype. Science. 2022 Mar 25;375(6587):eabm9609. PMID:35324283 doi:10.1126/science.abm9609
Student ContributorsStudent Contributors
- Ty Vander Eide
- Andrew Helmerich
- Ben Whiteside*