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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

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)

Function

Applications