[Putative molecular mechanism of defensin interaction with the membrane of the sensory neuron].
NP-1 defensin decreased effective charge transfer in the activation gating system of TTX-resistant (slow) sodium channels in a dose-dependent manner. The dissociation constant and Hill coefficient values were KD = 2 pM and X--0.9. Geometry of the NP-1 defensin molecule was built using its primary structure with three S-S briges and fully optimised in the framework of molecular mechanics method. The data obtained explain experimental results of stechiometry 1:1 due to ligand-receptor interaction by the only outward directed carboxyl group of Glu 14 which might form a hydrogen bond with a single binding site of non-identified defensin membrane receptor.
PLakhova
V B
VB
I. P. Pavlov Institute of Physiology, Russian Acad. Sci., 199034, St. Petersburg, Nab. Makarova, 6, Russia.
Shchegolev
B F
BF
Rogachevskiĭ
I V
IV
Nozdrachev
A D
AD
Krylov
B V
BV
Podzorova
S A
SA
Kokriakov
V N
VN
D000818:Animals; D002478:Cells, Cultured; D023082:Defensins / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D005727:Ganglia, Spinal / Q000166:cytology / Q000648:ultrastructure; D008564:Membrane Potentials; D008565:Membrane Proteins / Q000378:metabolism*; D008958:Models, Molecular; D009475:Neurons, Afferent / Q000187:drug effects / Q000378:metabolism* / Q000502:physiology; D051381:Rats; D017208:Rats, Wistar; D015222:Sodium Channels / Q000187:drug effects / Q000502:physiology; D013779:Tetrodotoxin / Q000494:pharmacology
D023082:Defensins; D008565:Membrane Proteins; D015222:Sodium Channels; D013779:Tetrodotoxin
Vozmozhnyĭ molekuliarnyĭ mekhanizm vzaimodeĭstviia defensina s membranoĭ sensornogo neĭrona]