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Structural insights into the assembly and substrate selectivity of human SPT–ORMDL3 complex

Structural insights into the assembly and substrate selectivity of human SPT–ORMDL3 complex

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_2487750198

Structural insights into the assembly and substrate selectivity of human SPT–ORMDL3 complex

About this item

Full title

Structural insights into the assembly and substrate selectivity of human SPT–ORMDL3 complex

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2021-03, Vol.28 (3), p.249-257

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

Human serine palmitoyltransferase (SPT) complex catalyzes the initial and rate-limiting step in the de novo biosynthesis of all sphingolipids. ORMDLs regulate SPT function, with human ORMDL3 being related to asthma. Here we report three high-resolution cryo-EM structures: the human SPT complex, composed of SPTLC1, SPTLC2 and SPTssa; the SPT–ORMDL3...

Alternative Titles

Full title

Structural insights into the assembly and substrate selectivity of human SPT–ORMDL3 complex

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_2487750198

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_2487750198

Other Identifiers

ISSN

1545-9993

E-ISSN

1545-9985

DOI

10.1038/s41594-020-00553-7

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