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Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for...

Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5490897

Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for Protein Translation

About this item

Full title

Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for Protein Translation

Publisher

United States: American Society of Plant Biologists

Journal title

Plant physiology (Bethesda), 2017-07, Vol.174 (3), p.1476-1491

Language

English

Formats

Publication information

Publisher

United States: American Society of Plant Biologists

More information

Scope and Contents

Contents

The association-dissociation of the cap-binding protein eukaryotic translation initiation factor 4E (eIF4E) with eIF4G is a key control step in eukaryotic translation. The paradigm on the eIF4E-eIF4G interaction states that eIF4G binds to the dorsal surface of eIF4E through a single canonical alpha-helical motif, while metazoan eIF4E-binding protei...

Alternative Titles

Full title

Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for Protein Translation

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5490897

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5490897

Other Identifiers

ISSN

0032-0889,1532-2548

E-ISSN

1532-2548

DOI

10.1104/pp.17.00193

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