Sandbox Reserved 482

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<Structure load='1KIL' size='500' frame='true' align='right' caption='Syntaxin-1A' scene='Insert optional scene name here' />
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<Structure load='1KIL' size='500' frame='true' align='right' caption='Syntaxin-1A - Three-dimensional structure of the complexin/SNARE complex.' scene='Insert optional scene name here' />
== Syntaxin-1A ==
== Syntaxin-1A ==
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[[Image:Syntaxincomplex.jpg]]
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This is the <scene name='Sandbox_Reserved_482/Syntaxin-1a/2'>active site</scene> of the protein.

Revision as of 21:16, 28 April 2012

This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500.
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Syntaxin-1A - Three-dimensional structure of the complexin/SNARE complex.

Drag the structure with the mouse to rotate

Syntaxin-1A

Image:Syntaxin-1A.png

Introduction

Syntaxin-1A is part of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family. It is an integrin plasma membrane protein found almost exclusively in neurons and it is known for its essential roles in neuronal signaling. (1) It assembles in tight core complexes, which promote fusion of carrier vesicles with target compartments. Members of the SNARE class of proteins are expressed in all eukaryotic cells and are distributed in distinct subcellular compartments. (2)


The neurodevelopmental disorder Williams syndrome is caused by the haploinsufficiency of genes. It is caused by deletion of genetic material. The deleted region has now been identified and syntaxin-1A is one of the genes that has been deleted. (3)


Structure

Syntaxin-1A has 288 residues. Residue 1-265 make up the cytoplasmic domain and residue 266-288 form the carboxyl-terminal transmembrane anchor. It adapts a well-folded tertiary structure with repeated hydrophobic residues forming a colied coil structure. (5)


NMR spectroscopy was used to identify a folded N-terminal domain in Syntaxin-1A and to determine its three-dimensional structure. This 120 residue N-terminal domain is conserved in plasma membrane syntaxins. The domain is made up from three long alpha helices and an up-and-down bundle with a left-handed twist. (4)

The image below is used to visualize the active site of the protein. It shows a neuronal synaptic fusion complex. SNARE proteins are involved in the fusion of vesicles with their target membranes but the structural details of these complexes are still unknown. X-ray is here used to show the crystal structure at 2.4 Å resolution of a core synaptic fusion complex containing syntaxin-1A, synaptobrevin-II and SNAP-25B. (6)

Image:Syntaxincomplex.jpg

This is the of the protein.


Mechanism of action

Applications

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