1nhl

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(New page: 200px<br /> <applet load="1nhl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nhl, resolution 2.3&Aring;" /> '''SNAP-23N Structure''...)
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Revision as of 16:15, 12 November 2007

Image:1nhl.gif

1nhl, resolution 2.3Å

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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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