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Crystal structure of MICU2 and comparison with MICU1 reveal insights into the uniporter gating mecha...

Crystal structure of MICU2 and comparison with MICU1 reveal insights into the uniporter gating mecha...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6397551

Crystal structure of MICU2 and comparison with MICU1 reveal insights into the uniporter gating mechanism

About this item

Full title

Crystal structure of MICU2 and comparison with MICU1 reveal insights into the uniporter gating mechanism

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2019-02, Vol.116 (9), p.3546-3555

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

The mitochondrial uniporter is a Ca2+-channel complex resident within the organelle’s inner membrane. In mammalian cells the uniporter’s activity is regulated by Ca2+ due to concerted action of MICU1 and MICU2, two paralogous, but functionally distinct, EF-hand Ca2+-binding proteins. Here we present the X-ray structure of the apo form of Mus muscul...

Alternative Titles

Full title

Crystal structure of MICU2 and comparison with MICU1 reveal insights into the uniporter gating mechanism

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6397551

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6397551

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1817759116

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