Log in to save to my catalogue

Structural basis for leucine-rich nuclear export signal recognition by CRM1

Structural basis for leucine-rich nuclear export signal recognition by CRM1

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3437623

Structural basis for leucine-rich nuclear export signal recognition by CRM1

About this item

Full title

Structural basis for leucine-rich nuclear export signal recognition by CRM1

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2009-04, Vol.458 (7242), p.1136-1141

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

CRM1 (also known as XPO1 and exportin 1) mediates nuclear export of hundreds of proteins through the recognition of the leucine-rich nuclear export signal (LR-NES). Here we present the 2.9 Å structure of CRM1 bound to snurportin 1 (SNUPN). Snurportin 1 binds CRM1 in a bipartite manner by means of an amino-terminal LR-NES and its nucleotide-binding...

Alternative Titles

Full title

Structural basis for leucine-rich nuclear export signal recognition by CRM1

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3437623

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3437623

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/nature07975

How to access this item