Abstract:
BACKGROUND:The eukaryotic voltage-gated sodium channel(e-Nav) is a large asymmetric transmembrane protein with important functions concerning neurological function. No structure has been resolved at high resolution for this protein. METHODS:A homology model of the transmembrane and extracellular regions of an Anopheles gambiae para-like channel with emphasis on the pore entrance has been constructed, based upon the templates provided by a prokaryotic sodium channel and a potassium two-pore channel. The latter provides a template for the extracellular regions, which are located above the entrance to the pore, which is likely to open at a side of a dome formed by these loops. RESULTS:A model created with this arrangement shows a structure similar to low-resolution cryoelectron microscope images of a related structure. The pore entrance also shows favorable electrostatic interface. CONCLUSION:Residues responsible for the negative charge around the pore have been traced in phylogeny to highlight their importance. This model is intended for the study of pore-blocking toxins.
journal_name
Curr Neuropharmacoljournal_title
Current neuropharmacologyauthors
Vinekar RS,Sowdhamini Rdoi
10.2174/1567201814666161205131213subject
Has Abstractpub_date
2017-11-14 00:00:00pages
1062-1072issue
8eissn
1570-159Xissn
1875-6190pii
CN-EPUB-80154journal_volume
15pub_type
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