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Allosteric signaling and dynamics of the clamshell-like NMDA receptor GluN1 N-terminal domain

Allosteric signaling and dynamics of the clamshell-like NMDA receptor GluN1 N-terminal domain

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_hal_primary_oai_HAL_hal_01498074v1

Allosteric signaling and dynamics of the clamshell-like NMDA receptor GluN1 N-terminal domain

About this item

Full title

Allosteric signaling and dynamics of the clamshell-like NMDA receptor GluN1 N-terminal domain

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2013-04, Vol.20 (4), p.477-485

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

NMDA receptors are heterotetrameric ligand-gated ion channels, with each subunit containing two extracellular clamshell-like domains. The dynamics of GluN1 NTD and its role in NMDA-receptor function are now explored by using functional and computational approaches. GluN1NTD is highly mobile and influences the gating and pharmacological profile of t...

Alternative Titles

Full title

Allosteric signaling and dynamics of the clamshell-like NMDA receptor GluN1 N-terminal domain

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_hal_primary_oai_HAL_hal_01498074v1

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_hal_primary_oai_HAL_hal_01498074v1

Other Identifiers

ISSN

1545-9993

E-ISSN

1545-9985

DOI

10.1038/nsmb.2522

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