1hvv
From Proteopedia
(New page: 200px<br /><applet load="1hvv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hvv, resolution 2.40Å" /> '''SELF-ASSOCIATION OF ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1hvv.gif|left|200px]]<br /><applet load="1hvv" size=" | + | [[Image:1hvv.gif|left|200px]]<br /><applet load="1hvv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hvv, resolution 2.40Å" /> | caption="1hvv, resolution 2.40Å" /> | ||
'''SELF-ASSOCIATION OF THE H3 REGION OF SYNTAXIN 1A: IMPLICATIONS FOR SNARE COMPLEX ASSEMBLY'''<br /> | '''SELF-ASSOCIATION OF THE H3 REGION OF SYNTAXIN 1A: IMPLICATIONS FOR SNARE COMPLEX ASSEMBLY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Intracellular membrane fusion requires SNARE proteins found on the vesicle | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1HVV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with TAR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1HVV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=TAR:'>TAR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HVV OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Misura, K | + | [[Category: Misura, K M.S.]] |
| - | [[Category: Scheller, R | + | [[Category: Scheller, R H.]] |
| - | [[Category: Weis, W | + | [[Category: Weis, W I.]] |
[[Category: TAR]] | [[Category: TAR]] | ||
[[Category: alpha-helix]] | [[Category: alpha-helix]] | ||
| Line 21: | Line 21: | ||
[[Category: homotetramer]] | [[Category: homotetramer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:29 2008'' |
Revision as of 11:05, 21 February 2008
|
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.
About this Structure
1HVV is a Single protein structure of sequence from Rattus norvegicus with as ligand. 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 Thu Feb 21 13:05:29 2008
