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Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon m...

Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon m...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5656675

Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding

About this item

Full title

Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding

Publisher

London: Nature Publishing Group UK

Journal title

Scientific reports, 2017-10, Vol.7 (1), p.14008-15, Article 14008

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

PROPPINs (β-propellers that bind polyphosphoinositides) are PtdIns3P and PtdIns(3,5)P
2
binding autophagy related proteins. They contain two phosphatidylinositolphosphate (PIP) binding sites and a conserved FRRG motif is essential for PIP binding. Here we present the 2.0 Å resolution crystal structure of the PROPPIN Atg18 from
Pichia angus...

Alternative Titles

Full title

Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5656675

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5656675

Other Identifiers

ISSN

2045-2322

E-ISSN

2045-2322

DOI

10.1038/s41598-017-14337-5

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