3c98: Difference between revisions

Revision as of 17:22, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3c98.png

Template:STRUCTURE 3c98

Revised structure of the munc18a-syntaxin1 complexRevised structure of the munc18a-syntaxin1 complex

Template:ABSTRACT PUBMED 18337752

About this StructureAbout this Structure

3C98 is a Protein complex structure of sequences from Rattus norvegicus. This structure supersedes the now removed PDB entry 1dn1. Full crystallographic information is available from OCA.

ReferenceReference

Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide., Burkhardt P, Hattendorf DA, Weis WI, Fasshauer D, EMBO J. 2008 Mar 13;. PMID:18337752

Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex., Misura KM, Scheller RH, Weis WI, Nature. 2000 Mar 23;404(6776):355-62. PMID:10746715

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OCA

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-'''Revised structure of the munc18a-syntaxin1 complex'''
+===Revised structure of the munc18a-syntaxin1 complex===
-==Overview==
+<!--
-Sec1/Munc18-like (SM) proteins functionally interact with SNARE proteins in vesicular fusion. Despite their high sequence conservation, structurally disparate binding modes for SM proteins with syntaxins have been observed. Several SM proteins appear to bind only to a short peptide present at the N terminus of syntaxin, designated the N-peptide, while Munc18a binds to a 'closed' conformation formed by the remaining portion of syntaxin 1a. Here, we show that the syntaxin 16 N-peptide binds to the SM protein Vps45, but the remainder of syntaxin 16 strongly enhances the affinity of the interaction. Likewise, the N-peptide of syntaxin 1a serves as a second binding site in the Munc18a/syntaxin 1a complex. When the syntaxin 1a N-peptide is bound to Munc18a, SNARE complex formation is blocked. Removal of the N-peptide enables binding of syntaxin 1a to its partner SNARE SNAP-25, while still bound to Munc18a. This suggests that Munc18a controls the accessibility of syntaxin 1a to its partners, a role that might be common to all SM proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_18337752}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18337752 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18337752}}
 ==About this Structure==
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 ==Reference==
 Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide., Burkhardt P, Hattendorf DA, Weis WI, Fasshauer D, EMBO J. 2008 Mar 13;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18337752 18337752]
+Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex., Misura KM, Scheller RH, Weis WI, Nature. 2000 Mar 23;404(6776):355-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10746715 10746715]
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 [[Category: Transmembrane]]
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