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Crystal structure of the Rab33B/Atg16L1 effector complex

Crystal structure of the Rab33B/Atg16L1 effector complex

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7395093

Crystal structure of the Rab33B/Atg16L1 effector complex

About this item

Full title

Crystal structure of the Rab33B/Atg16L1 effector complex

Publisher

London: Nature Publishing Group UK

Journal title

Scientific reports, 2020-07, Vol.10 (1), p.12956-12956, Article 12956

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The Atg12-Atg5/Atg16L1 complex is recruited by WIPI2b to the site of autophagosome formation. Atg16L1 is an effector of the Golgi resident GTPase Rab33B. Here we identified a minimal stable complex of murine Rab33B(30–202) Q92L and Atg16L1(153–210). Atg16L1(153–210) comprises the C-terminal part of the Atg16L1 coiled-coil domain. We have determined...

Alternative Titles

Full title

Crystal structure of the Rab33B/Atg16L1 effector complex

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7395093

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7395093

Other Identifiers

ISSN

2045-2322

E-ISSN

2045-2322

DOI

10.1038/s41598-020-69637-0

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