Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural dynamics at cytosolic interprotomer interfaces control gating of a mammalian TRPM5 channel.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 121, Issue 27, Page e2403333121, Year 2024
Publish date	Jul 2, 2024
Authors	Sebastian Karuppan / Lynn Goss Schrag / Caroline M Pastrano / Andrés Jara-Oseguera / Lejla Zubcevic /
PubMed Abstract	The transient receptor potential melastatin (TRPM) tetrameric cation channels are involved in a wide range of biological functions, from temperature sensing and taste transduction to regulation of ...The transient receptor potential melastatin (TRPM) tetrameric cation channels are involved in a wide range of biological functions, from temperature sensing and taste transduction to regulation of cardiac function, inflammatory pain, and insulin secretion. The structurally conserved TRPM cytoplasmic domains make up >70 % of the total protein. To investigate the mechanism by which the TRPM cytoplasmic domains contribute to gating, we employed electrophysiology and cryo-EM to study TRPM5-a channel that primarily relies on activation via intracellular Ca. Here, we show that activation of mammalian TRPM5 channels is strongly altered by Ca-dependent desensitization. Structures of rat TRPM5 identify a series of conformational transitions triggered by Ca binding, whereby formation and dissolution of cytoplasmic interprotomer interfaces appear to control activation and desensitization of the channel. This study shows the importance of the cytoplasmic assembly in TRPM5 channel function and sets the stage for future investigations of other members of the TRPM family.
External links	Proc Natl Acad Sci U S A / PubMed:38923985
Methods	EM (single particle)
Resolution	3.5 - 5.0 Å
Structure data	40574 8sl6 EMDB-40574, PDB-8sl6: Cryo-EM structure of the rat TRPM5 channel in EGTA Method: EM (single particle) / Resolution: 4.3 Å 40575 8sl8 EMDB-40575, PDB-8sl8: Cryo-EM structure of the rat TRPM5 channel in trace calcium, trace-1 Method: EM (single particle) / Resolution: 4.2 Å 40576 8sla EMDB-40576, PDB-8sla: Cryo-EM structure of the rat TRPM5 channel in trace calcium, trace-2 Method: EM (single particle) / Resolution: 3.7 Å 40577 8sle EMDB-40577, PDB-8sle: Cryo-EM structure of the rat TRPM5 channel in trace calcium, trace-3 Method: EM (single particle) / Resolution: 4.3 Å 40578 8sli EMDB-40578, PDB-8sli: Cryo-EM structure of the rat TRPM5 channel in 2mM calcium, high-1 Method: EM (single particle) / Resolution: 4.9 Å 40579 8slp EMDB-40579, PDB-8slp: Cryo-EM structure of the rat TRPM5 channel in 2mM calcium, high-2 Method: EM (single particle) / Resolution: 3.8 Å 40580 8slq EMDB-40580, PDB-8slq: Cryo-EM structure of the rat TRPM5 channel in 2mM calcium, high-3 Method: EM (single particle) / Resolution: 4.5 Å 40581 8slw EMDB-40581, PDB-8slw: Cryo-EM structure of the rat TRPM5 channel in 2mM calcium, high-4 Method: EM (single particle) / Resolution: 4.2 Å EMDB-40592: Focused map of the cytoplasmic domains of rat TRPM5, conformation high-4 Method: EM (single particle) / Resolution: 3.6 Å EMDB-40593: Focused map of the cytoplasmic domains of rat TRPM5, conformation high-3 Method: EM (single particle) / Resolution: 4.0 Å EMDB-40595: Focused map of the cytoplasmic domains of rat TRPM5, conformation high-2 Method: EM (single particle) / Resolution: 3.5 Å EMDB-40596: Focused map of the cytoplasmic domains of rat TRPM5, conformation high-1 Method: EM (single particle) / Resolution: 4.2 Å EMDB-40597: Focused map of the cytoplasmic domains of rat TRPM5, conformation trace-3 Method: EM (single particle) / Resolution: 5.0 Å EMDB-40599: Focused map of the cytoplasmic domains of rat TRPM5, conformation trace-2 Method: EM (single particle) / Resolution: 4.0 Å EMDB-40600: Focused map of the cytoplasmic domains of rat TRPM5, conformation trace-1 Method: EM (single particle) / Resolution: 4.4 Å
Chemicals	ChemComp-CA: Unknown entry
Source	rattus norvegicus (Norway rat)
Keywords	MEMBRANE PROTEIN / ion channel / Transient Receptor Potential / TRP / Transient Receptor Potential Melastatin 5 / TRPM5 / TRANSPORT PROTEIN