PXD035350

PXD035350 is an original dataset announced via ProteomeXchange.

Dataset Summary

Title	Structure of a volume-regulated heteromeric LRRC8A/C channel
Description	Volume-regulated anion channels participate in the cellular response to osmotic swelling. These membrane proteins are heteromers of LRRC8 family members whose composition determines permeation properties. Although structures of the obligatory LRRC8A subunit have previously defined the architecture of VRACs, the organization of heteromeric channels has remained elusive. Here we have closed this gap by the structural characterization of channels consisting of LRRC8A and C. Like homomeric LRRC8A, these proteins assemble as hexamers. Despite the twelve possible arrangements, we find a single predominant species with an A/C ratio of two. In this assembly, the four LRRCA subunits cluster in their preferred conformation observed in homomers as pairs of closely interacting proteins that stabilize a closed state of the channel. In contrast, the two interacting LRRC8C-subunits show a larger flexibility, underlining their role in the destabilization of the tightly packed A subunits, thereby enhancing the activation properties of the protein.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:12:31.434.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD035350
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Antje Dittmann
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	iodoacetamide derivatized residue
Instrument	Orbitrap Exploris 480

Dataset History

Revision	Datetime	Status	ChangeLog Entry
0	2022-07-14 07:38:54	ID requested
1	2023-01-04 03:50:12	announced
⏵ 2	2023-11-14 08:12:32	announced	2023-11-14: Updated project metadata.

Publication List

Rutz S, Deneka D, Dittmann A, Sawicka M, Dutzler R, Structure of a volume-regulated heteromeric LRRC8A/C channel. Nat Struct Mol Biol, 30(1):52-61(2023) [pubmed]
10.6019/PXD035350;

Rutz S, Deneka D, Dittmann A, Sawicka M, Dutzler R, Structure of a volume-regulated heteromeric LRRC8A/C channel. Nat Struct Mol Biol, 30(1):52-61(2023) [pubmed]

10.6019/PXD035350;

Keyword List

submitter keyword: LRRC8, cryo-EM, affinity purification, PRM, human, X-ray chrystallography, Exploris 480,Volume-regulated anion channels, nanobody

submitter keyword: LRRC8, cryo-EM, affinity purification, PRM, human, X-ray chrystallography, Exploris 480,Volume-regulated anion channels, nanobody

Contact List

Raimund Dutzler
contact affiliation	Department of Biochemistry University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland
contact email	dutzler@bioc.uzh.ch
lab head
Antje Dittmann
contact affiliation	ETH
contact email	antje.dittmann@gmail.com
dataset submitter

Full Dataset Link List

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2023/01/PXD035350
PRIDE project URI

Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2023/01/PXD035350

PRIDE project URI

Repository Record List

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