1ez3
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(New page: 200px<br /><applet load="1ez3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ez3, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 12:20, 20 November 2007
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CRYSTAL STRUCTURE OF THE NEURONAL T-SNARE SYNTAXIN-1A
Overview
Intracellular trafficking depends on the docking and fusion of transport, vesicles with cellular membranes. Central to docking and fusion is the, pairing of SNARE proteins (soluble NSF attachment protein receptors), associated with the vesicle and target membranes (v- and t-SNAREs, respectively). Here, the X-ray structure of an N-terminal conserved domain, of the neuronal t-SNARE syntaxin-1A was determined to a resolution of 1.9, A using multiwavelength anomalous diffraction. This X-ray structure, which, is in general agreement with an NMR structure of a similar fragment, provides new insight into the interaction surface between the N-terminal, domain and the remainder of the protein. In vitro characterization of the, intact cytoplasmic domain of syntaxin revealed that it forms dimers, and, probably tetramers, at low micromolar concentrations, with concomitant, structural changes that can be detected by limited proteolysis. These, observations suggest that the promiscuity characteristic of pairing, between v-SNAREs and t-SNAREs extends to the formation of homo-oligomeric, t-SNARE complexes as well. They also suggest a potential role for the, neuronal Sec1 protein (nSec1) in preventing the formation of syntaxin, multimers.
About this Structure
1EZ3 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural analysis of the neuronal SNARE protein syntaxin-1A., Lerman JC, Robblee J, Fairman R, Hughson FM, Biochemistry. 2000 Jul 25;39(29):8470-9. PMID:10913252
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