1hs7: Difference between revisions

Revision as of 08:36, 1 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:1hs7.png

Template:STRUCTURE 1hs7

VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTUREVAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE

Template:ABSTRACT PUBMED 11224573

About this StructureAbout this Structure

1HS7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.

ReferenceReference

Vam3p structure reveals conserved and divergent properties of syntaxins., Dulubova I, Yamaguchi T, Wang Y, Sudhof TC, Rizo J, Nat Struct Biol. 2001 Mar;8(3):258-64. PMID:11224573

Page seeded by OCA on Tue Jul 1 08:36:45 2008

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 {{STRUCTURE_1hs7|  PDB=1hs7  |  SCENE=  }}
-'''VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE'''
+===VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE===
-==Overview==
+<!--
-Syntaxins and Sec1/munc18 proteins are central to intracellular membrane fusion. All syntaxins comprise a variable N-terminal region, a conserved SNARE motif that is critical for SNARE complex formation, and a transmembrane region. The N-terminal region of neuronal syntaxin 1A contains a three-helix domain that folds back onto the SNARE motif forming a 'closed' conformation; this conformation is required for munc18-1 binding. We have examined the generality of the structural properties of syntaxins by NMR analysis of Vam3p, a yeast syntaxin essential for vacuolar fusion. Surprisingly, Vam3p also has an N-terminal three-helical domain despite lacking apparent sequence homology with syntaxin 1A in this region. However, Vam3p does not form a closed conformation and its N-terminal domain is not required for binding to the Sec1/munc18 protein Vps33p, suggesting that critical distinctions exist in the mechanisms used by syntaxins to govern different types of membrane fusion.
+The line below this paragraph, {{ABSTRACT_PUBMED_11224573}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11224573 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11224573}}
 ==About this Structure==
-HS7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HS7 OCA].
+HS7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HS7 OCA].
 ==Reference==
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 [[Category: Yamaguchi, T.]]
 [[Category: Up-and-down three-helix bundle insertion preceding proline in an alpha-helix]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:36:45 2008''