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Heat-dependent opening of TRPV1 in the presence of capsaicin

Heat-dependent opening of TRPV1 in the presence of capsaicin

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8335751

Heat-dependent opening of TRPV1 in the presence of capsaicin

About this item

Full title

Heat-dependent opening of TRPV1 in the presence of capsaicin

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2021-07, Vol.28 (7), p.554-563

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

Transient receptor potential vanilloid member 1 (TRPV1) is a Ca
2+
-permeable cation channel that serves as the primary heat and capsaicin sensor in humans. Using cryo-EM, we have determined the structures of apo and capsaicin-bound full-length rat TRPV1 reconstituted into lipid nanodiscs over a range of temperatures. This has allowed us to v...

Alternative Titles

Full title

Heat-dependent opening of TRPV1 in the presence of capsaicin

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8335751

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8335751

Other Identifiers

ISSN

1545-9993

E-ISSN

1545-9985

DOI

10.1038/s41594-021-00616-3

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