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Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide bin...

Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide bin...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pnas_primary_104_21_8773

Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide binding mode of Sec1/Munc18 proteins

About this item

Full title

Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide binding mode of Sec1/Munc18 proteins

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2007-05, Vol.104 (21), p.8773-8778

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Sec1/Munc18 proteins (SM proteins) bind to soluble NSF attachment protein receptors (SNAREs) and play an essential role in membrane fusion. Divergent modes of regulation have been proposed for different SM proteins indicating that they can either promote or inhibit SNARE assembly. This is in part because of discrete modes of binding that have been...

Alternative Titles

Full title

Structure of the Munc18c/Syntaxin4 N-peptide complex defines universal features of the N-peptide binding mode of Sec1/Munc18 proteins

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pnas_primary_104_21_8773

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pnas_primary_104_21_8773

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0701124104

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