Source:http://linkedlifedata.com/resource/pubmed/id/12556468
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
2003-4-7
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pubmed:databankReference | |
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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Qb-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Qc-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNAP23 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13462-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12556468-Amino Acid Sequence,
pubmed-meshheading:12556468-Animals,
pubmed-meshheading:12556468-Carrier Proteins,
pubmed-meshheading:12556468-Crystallography, X-Ray,
pubmed-meshheading:12556468-Humans,
pubmed-meshheading:12556468-Macromolecular Substances,
pubmed-meshheading:12556468-Models, Molecular,
pubmed-meshheading:12556468-Molecular Sequence Data,
pubmed-meshheading:12556468-Polymerase Chain Reaction,
pubmed-meshheading:12556468-Protein Conformation,
pubmed-meshheading:12556468-Protein Structure, Secondary,
pubmed-meshheading:12556468-Qb-SNARE Proteins,
pubmed-meshheading:12556468-Qc-SNARE Proteins,
pubmed-meshheading:12556468-Recombinant Proteins,
pubmed-meshheading:12556468-Sequence Alignment,
pubmed-meshheading:12556468-Sequence Homology, Amino Acid
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pubmed:year |
2003
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pubmed:articleTitle |
Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain.
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pubmed:affiliation |
Division of Hemostasis and Thrombosis, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02115, USA. sfreedm2@caregroup.harvard.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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