Structure of an AMPK complex in an inactive, ATP-bound state.
Posted on April 3, 2023
Title | Structure of an AMPK complex in an inactive, ATP-bound state. |
Publication Type | Journal Article |
Authors | Yan, Yan, Mukherjee Somnath, Harikumar Kaleeckal G., Strutzenberg Timothy S., X Zhou Edward, Suino-Powell Kelly, Xu Ting-Hai, Sheldon Ryan D., Lamp Jared, Brunzelle Joseph S., Radziwon Katarzyna, Ellis Abigail, Novick Scott J., Vega Irving E., Jones Russell G., Miller Laurence J., H Xu Eric, Griffin Patrick R., Kossiakoff Anthony A., and Melcher Karsten |
PubMed ID | 34437114 |
PubMed Central ID | PMC8428800 |
Grant List | R01 GM117372 / GM / NIGMS NIH HHS / United States R01 GM129436 / GM / NIGMS NIH HHS / United States |
Publications
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- Development of a universal nanobody-binding Fab module for fiducial-assisted cryo-EM studies of membrane proteins.
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- Isoform- and ligand-specific modulation of the adhesion GPCR ADGRL3/Latrophilin3 by a synthetic binder.
- Quaternary structure independent folding of voltage-gated ion channel pore domain subunits.
- Structural basis for assembly and lipid-mediated gating of LRRC8A:C volume-regulated anion channels.
- Structure of an AMPK complex in an inactive, ATP-bound state.
- Structure of human NTCP reveals the basis of recognition and sodium-driven transport of bile salts into the liver.
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- Synthetic Antibodies Detect Distinct Cellular States of Chromosome Passenger Complex Proteins.
- Targeting a proteolytic neoepitope on CUB domain containing protein 1 (CDCP1) for RAS-driven cancers.
RAN Publications
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Conformation-specific Synthetic Antibodies Discriminate Multiple Functional States of the Ion Channel CorA. (published on 2023 Jul 01)
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Structural basis for assembly and lipid-mediated gating of LRRC8A:C volume-regulated anion channels. (published on 2023 Mar 16)