1hvv: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1hvv.gif|left|200px]]
{{Seed}}
[[Image:1hvv.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hvv|  PDB=1hvv  |  SCENE=  }}  
{{STRUCTURE_1hvv|  PDB=1hvv  |  SCENE=  }}  


'''SELF-ASSOCIATION OF THE H3 REGION OF SYNTAXIN 1A: IMPLICATIONS FOR SNARE COMPLEX ASSEMBLY'''
===SELF-ASSOCIATION OF THE H3 REGION OF SYNTAXIN 1A: IMPLICATIONS FOR SNARE COMPLEX ASSEMBLY===




==Overview==
<!--
Intracellular membrane fusion requires SNARE proteins found on the vesicle and target membranes. SNAREs associate by formation of a parallel four-helix bundle, and it has been suggested that formation of this complex promotes membrane fusion. The membrane proximal region of the cytoplasmic domain of the SNARE syntaxin 1A, designated H3, contributes one of the four helices to the SNARE complex. In the crystal structure of syntaxin 1A H3, four molecules associate as a homotetramer composed of two pairs of parallel helices that are anti-parallel to each other. The H3 oligomer observed in the crystals is also found in solution, as assessed by gel filtration and chemical cross-linking studies. The crystal structure reveals that the highly conserved Phe-216 packs against conserved Gln-226 residues present on the anti-parallel pair of helices. Modeling indicates that Phe-216 prevents parallel tetramer formation. Mutation of Phe-216 to Leu appears to allow formation of parallel tetramers, whereas mutation to Ala destabilizes the protein. These results indicate that Phe-216 has a role in preventing formation of stable parallel helical bundles, thus favoring the interaction of the H3 region of syntaxin 1a with other proteins involved in membrane fusion.
The line below this paragraph, {{ABSTRACT_PUBMED_11118447}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11118447 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11118447}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Four-helix bundle]]
[[Category: Four-helix bundle]]
[[Category: Homotetramer]]
[[Category: Homotetramer]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:16:56 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:53:17 2008''

Revision as of 05:53, 1 July 2008

File:1hvv.png

Template:STRUCTURE 1hvv

SELF-ASSOCIATION OF THE H3 REGION OF SYNTAXIN 1A: IMPLICATIONS FOR SNARE COMPLEX ASSEMBLY

Template:ABSTRACT PUBMED 11118447

About this Structure

1HVV is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Self-association of the H3 region of syntaxin 1A. Implications for intermediates in SNARE complex assembly., Misura KM, Scheller RH, Weis WI, J Biol Chem. 2001 Apr 20;276(16):13273-82. Epub 2000 Dec 15. PMID:11118447

Page seeded by OCA on Tue Jul 1 08:53:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1hvv&oldid=609002"