| pubmed-article:12556468 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12556468 | lifeskim:mentions | umls-concept:C1516692 | lld:lifeskim |
| pubmed-article:12556468 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12556468 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:12556468 | pubmed:dateCreated | 2003-4-7 | lld:pubmed |
| pubmed-article:12556468 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12556468 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:12556468 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12556468 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12556468 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12556468 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:12556468 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12556468 | pubmed:author | pubmed-author:SongHyun... | lld:pubmed |
| pubmed-article:12556468 | pubmed:author | pubmed-author:EckMichael... | lld:pubmed |
| pubmed-article:12556468 | pubmed:author | pubmed-author:SunZhen-Yu... | lld:pubmed |
| pubmed-article:12556468 | pubmed:author | pubmed-author:FreedmanSteve... | lld:pubmed |
| pubmed-article:12556468 | pubmed:author | pubmed-author:XuYingwuY | lld:pubmed |
| pubmed-article:12556468 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12556468 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:12556468 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12556468 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12556468 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12556468 | pubmed:pagination | 13462-7 | lld:pubmed |
| pubmed-article:12556468 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12556468 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12556468 | pubmed:articleTitle | Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain. | lld:pubmed |
| pubmed-article:12556468 | pubmed:affiliation | Division of Hemostasis and Thrombosis, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02115, USA. sfreedm2@caregroup.harvard.edu | lld:pubmed |
| pubmed-article:12556468 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12556468 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12556468 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12556468 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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