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PMID: 12496247 Published · ppublish English Journal Article

High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex.

The Journal of biological chemistry ·Vol. 278 ·No. 10 ·2003-03-07 ·Pages 8630-6

Ernst JA, Brunger AT

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
Amino Acid Sequence Animals Biopolymers Calcium-Binding Proteins Circular Dichroism Crystallography, X-Ray Membrane Glycoproteins/metabolism Membrane Proteins/chemistry,genetics,metabolism Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Nerve Tissue Proteins/metabolism Neurons/metabolism Protein Binding Protein Conformation Rats SNARE Proteins Sequence Homology, Amino Acid Synaptotagmin I Synaptotagmins Vesicular Transport Proteins
Chemicals
Biopolymers Calcium-Binding Proteins Membrane Glycoproteins Membrane Proteins Nerve Tissue Proteins SNARE Proteins Synaptotagmin I Syt1 protein, rat Vesicular Transport Proteins Synaptotagmins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ernst James A
Howard Hughes Medical Institute, Stanford University, California 94305, USA.
Brunger Axel T
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2003-03-07
Epub
2002-00-20
Pages
8630-6
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Databases
PDB
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