Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cryo-EM structure of the TMEM16A in Nanodisc

ABSTRACT:

SUBMITTER: Shangyu Dang

PROVIDER: EMPIAR-10123 | biostudies-other |

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Publications

Cryo-EM structures of the TMEM16A calcium-activated chloride channel.

Dang Shangyu S Feng Shengjie S Tien Jason J Peters Christian J CJ Bulkley David D Lolicato Marco M Zhao Jianhua J Zuberbühler Kathrin K Ye Wenlei W Qi Lijun L Chen Tingxu T Craik Charles S CS Jan Yuh Nung YN Minor Daniel L DL Cheng Yifan Y Jan Lily Yeh LY

Nature 20171213 7685

Calcium-activated chloride channels (CaCCs) encoded by TMEM16A control neuronal signalling, smooth muscle contraction, airway and exocrine gland secretion, and rhythmic movements of the gastrointestinal system. To understand how CaCCs mediate and control anion permeation to fulfil these physiological functions, knowledge of the mammalian TMEM16A structure and identification of its pore-lining residues are essential. TMEM16A forms a dimer with two pores. Previous CaCC structural analyses have rel ...[more]

PMID: 29236684

Similar Datasets

Cryo-EM structure of the TMEM16A in LMNG

Project description: Not available

| EMPIAR-10124 | biostudies-other

Cryo-EM structure of TRPV5 W583A in nanodisc

Project description: Not available

| EMPIAR-10253 | biostudies-other

Cryo-EM structures of the TMEM16A calcium-activated chloride channel.

Project description:Calcium-activated chloride channels (CaCCs) encoded by TMEM16A control neuronal signalling, smooth muscle contraction, airway and exocrine gland secretion, and rhythmic movements of the gastrointestinal system. To understand how CaCCs mediate and control anion permeation to fulfil these physiological functions, knowledge of the mammalian TMEM16A structure and identification of its pore-lining residues are essential. TMEM16A forms a dimer with two pores. Previous CaCC structural analyses have relied on homology modelling of a homologue (nhTMEM16) from the fungus Nectria haematococca that functions primarily as a lipid scramblase, as well as subnanometre-resolution electron cryo-microscopy. Here we present de novo atomic structures of the transmembrane domains of mouse TMEM16A in nanodiscs and in lauryl maltose neopentyl glycol as determined by single-particle electron cryo-microscopy. These structures reveal the ion permeation pore and represent different functional states. The structure in lauryl maltose neopentyl glycol has one Ca2+ ion resolved within each monomer with a constricted pore; this is likely to correspond to a closed state, because a CaCC with a single Ca2+ occupancy requires membrane depolarization in order to open (C.J.P. et al., manuscript submitted). The structure in nanodiscs has two Ca2+ ions per monomer and its pore is in a closed conformation; this probably reflects channel rundown, which is the gradual loss of channel activity that follows prolonged CaCC activation in 1?mM Ca2+. Our mutagenesis and electrophysiological studies, prompted by analyses of the structures, identified ten residues distributed along the pore that interact with permeant anions and affect anion selectivity, as well as seven pore-lining residues that cluster near pore constrictions and regulate channel gating. Together, these results clarify the basis of CaCC anion conduction.

| S-EPMC5750132 | biostudies-literature

Cryo-EM structure of TRPV5 full length in nanodisc

Project description: Not available

| EMPIAR-10254 | biostudies-other

Cryo-EM structure of TRPV5 1-660 in nanodisc

Project description: Not available

| EMPIAR-10255 | biostudies-other

Cryo-EM structure of mouse TRPV3 in a nanodisc

Project description: Not available

| EMPIAR-10400 | biostudies-other

Cryo-EM structure of cell-free synthesized human histamine 2 receptor/G<sub>s</sub> complex in nanodisc environment.

Project description:Here we describe the cryo-electron microscopy structure of the human histamine 2 receptor (H2R) in an active conformation with bound histamine and in complex with Gs heterotrimeric protein at an overall resolution of 3.4 Å. The complex was generated by cotranslational insertion of the receptor into preformed nanodisc membranes using cell-free synthesis in E. coli lysates. Structural comparison with the inactive conformation of H2R and the inactive and Gq-coupled active state of H1R together with structure-guided functional experiments reveal molecular insights into the specificity of ligand binding and G protein coupling for this receptor family. We demonstrate lipid-modulated folding of cell-free synthesized H2R, its agonist-dependent internalization and its interaction with endogenously synthesized H1R and H2R in HEK293 cells by applying a recently developed nanotransfer technique.

| S-EPMC10901899 | biostudies-literature

Cryo-EM structure of SETD2/Set2 methyltransferase bound to a nucleosome containing oncohistone mutations

Project description:Setd2 methylate the nucleosome to form H3K36me3. Here we utilized the Cryo-EM to elucidate the structure of SETD2/Set2 bound with nucleosomes. Through this structure analysis, we found that histone H1 may interfere the enzymatic activity of SETD2/Set2 by inhibiting their binding affinity.

2021-05-20 | GSE148235 | GEO

Cryo-EM structure of calcium-bound TMEM16F in nanodisc with supplement of PIP2

Project description: Not available

| EMPIAR-10280 | biostudies-other

Atomic Resolution Cryo-EM Structure of ?-Galactosidase.

Project description:The advent of direct electron detectors has enabled the routine use of single-particle cryo-electron microscopy (EM) approaches to determine structures of a variety of protein complexes at near-atomic resolution. Here, we report the development of methods to account for local variations in defocus and beam-induced drift, and the implementation of a data-driven dose compensation scheme that significantly improves the extraction of high-resolution information recorded during exposure of the specimen to the electron beam. These advances enable determination of a cryo-EM density map for ?-galactosidase bound to the inhibitor phenylethyl ?-D-thiogalactopyranoside where the ordered regions are resolved at a level of detail seen in X-ray maps at ? 1.5 Å resolution. Using this density map in conjunction with constrained molecular dynamics simulations provides a measure of the local flexibility of the non-covalently bound inhibitor and offers further opportunities for structure-guided inhibitor design.

| S-EPMC6129192 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data