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	Conformational trajectory of allosteric gating of the human cone photoreceptor cyclic nucleotide-gated channel.
Journal, issue, pages	Nat Commun, Vol. 14, Issue 1, Page 4284, Year 2023
Publish date	Jul 18, 2023
Authors	Zhengshan Hu / Xiangdong Zheng / Jian Yang /
PubMed Abstract	Cyclic nucleotide-gated (CNG) channels transduce chemical signals into electrical signals in sensory receptors and neurons. They are activated by cGMP or cAMP, which bind to the cyclic nucleotide- ...Cyclic nucleotide-gated (CNG) channels transduce chemical signals into electrical signals in sensory receptors and neurons. They are activated by cGMP or cAMP, which bind to the cyclic nucleotide-binding domain (CNBD) to open a gate located 50-60 Å away in the central cavity. Structures of closed and open vertebrate CNG channels have been solved, but the conformational landscape of this allosteric gating remains to be elucidated and enriched. Here, we report structures of the cGMP-activated human cone photoreceptor CNGA3/CNGB3 channel in closed, intermediate, pre-open and open states in detergent or lipid nanodisc, all with fully bound cGMP. The pre-open and open states are obtained only in the lipid nanodisc, suggesting a critical role of lipids in tuning the energetic landscape of CNGA3/CNGB3 activation. The different states exhibit subunit-unique, incremental and distinct conformational rearrangements that originate in the CNBD, propagate through the gating ring to the transmembrane domain, and gradually open the S6 cavity gate. Our work illustrates a spatial conformational-change wave of allosteric gating of a vertebrate CNG channel by its natural ligand and provides an expanded framework for studying CNG properties and channelopathy.
External links	Nat Commun / PubMed:37463923 / PubMed Central
Methods	EM (single particle)
Resolution	3.11 - 3.62 Å
Structure data	28595 8etp EMDB-28595, PDB-8etp: Cryo-EM structure of cGMP bound closed state of human CNGA3/CNGB3 channel in GDN Method: EM (single particle) / Resolution: 3.52 Å 28603 8eu3 EMDB-28603, PDB-8eu3: Cryo-EM structure of cGMP bound human CNGA3/CNGB3 channel in GDN, transition state 1 Method: EM (single particle) / Resolution: 3.62 Å 28611 8euc EMDB-28611, PDB-8euc: Cryo-EM structure of cGMP bound human CNGA3/CNGB3 channel in GDN, transition state 2 Method: EM (single particle) / Resolution: 3.61 Å 28622 8ev8 EMDB-28622, PDB-8ev8: Cryo-EM structure of cGMP bound truncated human CNGA3/CNGB3 channel in lipid nanodisc, closed state Method: EM (single particle) / Resolution: 3.11 Å 28623 8ev9 EMDB-28623, PDB-8ev9: Cryo-EM structure of cGMP bound truncated human CNGA3/CNGB3 channel in lipid nanodisc, transition state 1 Method: EM (single particle) / Resolution: 3.33 Å 28624 8eva EMDB-28624, PDB-8eva: Cryo-EM structure of cGMP bound truncated human CNGA3/CNGB3 channel in lipid nanodisc, transition state 2 Method: EM (single particle) / Resolution: 3.33 Å 28625 8evb EMDB-28625, PDB-8evb: Cryo-EM structure of cGMP bound truncated human CNGA3/CNGB3 channel in lipid nanodisc, pre-open state Method: EM (single particle) / Resolution: 3.6 Å 28626 8evc EMDB-28626, PDB-8evc: Cryo-EM structure of cGMP bound truncated human CNGA3/CNGB3 channel in lipid nanodisc, open state Method: EM (single particle) / Resolution: 3.33 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine ChemComp-PCG: CYCLIC GUANOSINE MONOPHOSPHATE / Cyclic guanosine monophosphate
Source	homo sapiens (human)
Keywords	MEMBRANE PROTEIN / Heterotetramer / ligand-bound / ligand-gated / ion channel / CNGA3 / CNGB3