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1nhl

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==Overview==
==Overview==
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SNARE proteins mediate intracellular membrane fusion by forming a, coiled-coil complex to merge opposing membranes. A "fusion-active", neuronal SNARE complex is a parallel four-helix bundle containing two, coiled-coil domains from SNAP-25 and one coiled-coil domain each from, syntaxin-1a and VAMP-2. "Prefusion" assembly intermediate complexes can, also form from these SNAREs. We studied the N-terminal coiled-coil domain, of SNAP-23 (SNAP-23N), a non-neuronal homologue of SNAP-25, and its, interaction with other coiled-coil domains. SNAP-23N can assemble, spontaneously with the coiled-coil domains from SNAP-23C, syntaxin-4, and, VAMP-3 to form a heterotetrameric complex. Unexpectedly, pure SNAP-23N, crystallizes as a coiled-coil homotetrameric complex. The four helices, have a parallel orientation and are symmetrical about the long axis. The, complex is stabilized through the interaction of conserved hydrophobic, residues comprising the a and d positions of the coiled-coil heptad, repeats. In addition, a central, highly conserved glutamine residue, (Gln-48) is buried within the interface by hydrogen bonding between, glutamine side chains derived from adjacent subunits and to solvent, molecules. A comparison of the SNAP-23N structure to other SNARE complex, structures reveals how a simple coiled-coil motif can form diverse SNARE, complexes.
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SNARE proteins mediate intracellular membrane fusion by forming a coiled-coil complex to merge opposing membranes. A "fusion-active" neuronal SNARE complex is a parallel four-helix bundle containing two coiled-coil domains from SNAP-25 and one coiled-coil domain each from syntaxin-1a and VAMP-2. "Prefusion" assembly intermediate complexes can also form from these SNAREs. We studied the N-terminal coiled-coil domain of SNAP-23 (SNAP-23N), a non-neuronal homologue of SNAP-25, and its interaction with other coiled-coil domains. SNAP-23N can assemble spontaneously with the coiled-coil domains from SNAP-23C, syntaxin-4, and VAMP-3 to form a heterotetrameric complex. Unexpectedly, pure SNAP-23N crystallizes as a coiled-coil homotetrameric complex. The four helices have a parallel orientation and are symmetrical about the long axis. The complex is stabilized through the interaction of conserved hydrophobic residues comprising the a and d positions of the coiled-coil heptad repeats. In addition, a central, highly conserved glutamine residue (Gln-48) is buried within the interface by hydrogen bonding between glutamine side chains derived from adjacent subunits and to solvent molecules. A comparison of the SNAP-23N structure to other SNARE complex structures reveals how a simple coiled-coil motif can form diverse SNARE complexes.
==About this Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Eck, M.J.]]
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[[Category: Eck, M J.]]
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[[Category: Freedman, S.J.]]
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[[Category: Freedman, S J.]]
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[[Category: Song, H.K.]]
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[[Category: Song, H K.]]
[[Category: Xu, Y.]]
[[Category: Xu, Y.]]
[[Category: coiled-coil]]
[[Category: coiled-coil]]
[[Category: snare]]
[[Category: snare]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:29:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:11 2008''

Revision as of 12:06, 21 February 2008

Image:1nhl.jpg

1nhl, resolution 2.3Å

Drag the structure with the mouse to rotate

SNAP-23N Structure

Overview

SNARE proteins mediate intracellular membrane fusion by forming a coiled-coil complex to merge opposing membranes. A "fusion-active" neuronal SNARE complex is a parallel four-helix bundle containing two coiled-coil domains from SNAP-25 and one coiled-coil domain each from syntaxin-1a and VAMP-2. "Prefusion" assembly intermediate complexes can also form from these SNAREs. We studied the N-terminal coiled-coil domain of SNAP-23 (SNAP-23N), a non-neuronal homologue of SNAP-25, and its interaction with other coiled-coil domains. SNAP-23N can assemble spontaneously with the coiled-coil domains from SNAP-23C, syntaxin-4, and VAMP-3 to form a heterotetrameric complex. Unexpectedly, pure SNAP-23N crystallizes as a coiled-coil homotetrameric complex. The four helices have a parallel orientation and are symmetrical about the long axis. The complex is stabilized through the interaction of conserved hydrophobic residues comprising the a and d positions of the coiled-coil heptad repeats. In addition, a central, highly conserved glutamine residue (Gln-48) is buried within the interface by hydrogen bonding between glutamine side chains derived from adjacent subunits and to solvent molecules. A comparison of the SNAP-23N structure to other SNARE complex structures reveals how a simple coiled-coil motif can form diverse SNARE complexes.

About this Structure

1NHL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain., Freedman SJ, Song HK, Xu Y, Sun ZY, Eck MJ, J Biol Chem. 2003 Apr 11;278(15):13462-7. Epub 2003 Jan 29. PMID:12556468

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