Sandbox Reserved 482

• Click the edit this page tab at the top. Save the page after each step, then edit it again.
• Click the 3D button (when editing, above the wikitext box) to insert Jmol.
• show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
• Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

For more help, look at this link: http://www.proteopedia.org/wiki/index.php/Help:Getting_Started_in_Proteopedia

Syntaxin-1A

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

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)

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)

Function

Applications