1hs7: Difference between revisions

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[[Image:1hs7.gif|left|200px]]
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{{STRUCTURE_1hs7|  PDB=1hs7  |  SCENE=  }}  
{{STRUCTURE_1hs7|  PDB=1hs7  |  SCENE=  }}  


'''VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE'''
===VAM3P N-TERMINAL DOMAIN SOLUTION STRUCTURE===




==Overview==
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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.
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==About this Structure==
==About this Structure==
1HS7 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].  
1HS7 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==
==Reference==
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[[Category: Yamaguchi, T.]]
[[Category: Yamaguchi, T.]]
[[Category: Up-and-down three-helix bundle insertion preceding proline in an alpha-helix]]
[[Category: Up-and-down three-helix bundle insertion preceding proline in an alpha-helix]]
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