Cryo-EM structure of the polycystin 2-l1 ion channel
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Summary
The near atomic resolution (3.1 Å) of the polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel is reported and it is shown that the differences in sequence similarity and permeability are reflected in the architecture of polycyst in 2- l1.
- Type
- article
- Published
- 2018-03-22
- Cited by
- 46
- References
- 40
- Access
- Open access
- OpenAlex
- https://openalex.org/W2789369294
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:261833682
Keywords
Cilium, Polycystic kidney disease, Ion channel, PKD1, Chemistry
References
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Cited by
- Autosomal dominant PKD gets an atomic map
- A hypothetical molecular mechanism for TRPV1 activation that invokes rotation of an S6 asparagine
- Purification of Functional Human TRP Channels Recombinantly Produced in Yeast
- Molecular Structure of the PKD Protein Complex Finally Solved.
- Lipid Interactions of a Ciliary Membrane TRP Channel: Simulation and Structural Studies of Polycystin-2 (PC2)
- Structure and function of polycystins: insights into polycystic kidney disease
- Transient Receptor Potential Channels and Calcium Signaling.
- The role of calmodulin in regulating calcium-permeable PKD2L1 channel activity
- Opening TRPP2 (PKD2L1) requires the transfer of gating charges
- The cilium as a force sensor−myth versus reality
- The role of π-helices in TRP channel gating
- Lipid Interactions of a Ciliary Membrane TRP Channel: Simulation and Structural Studies of Polycystin-2
- An overview on transient receptor potential channels superfamily.
- Structure and function of polycystin channels in primary cilia
- Molecular dysregulation of ciliary polycystin-2 channels caused by variants in the TOP domain
- Ca2+/calmodulin-dependent regulation of polycystic kidney disease 2-like-1 by binding at C-terminal domain
- Global alignment and assessment of TRP channel transmembrane domain structures to explore functional mechanisms
- Current approaches for automated model building into cryo-EM maps using Buccaneer with CCP-EM
- TranSPHIRE: automated and feedback-optimized on-the-fly processing for cryo-EM
- Structural basis of TRPC4 regulation by calmodulin and pharmacological agents
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