Andrew Helmerich Sandbox 1: Difference between revisions
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<scene name='10/1038819/18-25_of_chain_a/8'>TextToBeDisplayed</scene> | <scene name='10/1038819/18-25_of_chain_a/8'>TextToBeDisplayed</scene> | ||
== Amidated C-Terminus | == Amidated C-Terminus == | ||
<scene name='10/1038819/Amidated_c_term/1'>Amidated C-Terminus</scene> | <scene name='10/1038819/Amidated_c_term/1'>Amidated C-Terminus</scene> | ||
Revision as of 16:02, 4 April 2024
The Amylin Receptor: A Unique GPCRThe Amylin Receptor: A Unique GPCR
IntroductionOverview and FunctionRole of Amylinxx
Amidated C-Terminus
DiseaseRelevanceStructural 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*