Abstract
The structure of a truncated SNARE complex has been solved to 1.4-A resolution revealing a stabilizing salt bridge, sites of hydration, and conformational variability of the ionic central layer that were not observed in a previously published structure at 2.4-A resolution (Sutton, R. B., Fasshauer, D., Jahn, R., and Brunger, A. T. (1998) Nature 395, 347-353). The truncated complex lacks residues involved in phospholipid binding and denatures at a lower temperature than longer complexes as assessed by SDS and circular dichroism thermal melts. The truncated SNARE complex is monomeric, and it retains binding to synaptotagmin I.
MeSH terms
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Amino Acid Sequence
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Animals
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Biopolymers
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Calcium-Binding Proteins*
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Circular Dichroism
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Crystallography, X-Ray
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Membrane Glycoproteins / metabolism*
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Membrane Proteins / chemistry
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Nerve Tissue Proteins / metabolism*
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Neurons / metabolism*
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Protein Binding
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Protein Conformation
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Rats
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SNARE Proteins
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Sequence Homology, Amino Acid
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Synaptotagmin I
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Synaptotagmins
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Vesicular Transport Proteins*
Substances
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Biopolymers
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Calcium-Binding Proteins
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Membrane Glycoproteins
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Membrane Proteins
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Nerve Tissue Proteins
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SNARE Proteins
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Synaptotagmin I
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Syt1 protein, rat
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Vesicular Transport Proteins
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Synaptotagmins