tailieunhanh - Báo cáo Y học: Variations in receptor site-3 on rat brain and insect sodium channels highlighted by binding of a funnel-web spider d-atracotoxin

d-Atracotoxins (d-ACTXs) from Australian funnel-web spiders differ structurally from scorpion a-toxins (ScaTx) but similarly slow sodium current inactivation and compete for their binding to sodium channels at receptor site-3. Characterization of the binding of 125 I-labelled d-ACTX-Hv1a to various sodium channels reveals a decrease in a nity for depolarized (0 mV;Kd nM) ()55 mV;Kd ) rat brain synaptosomes. | Eur. J. Biochem. 269 1500-1510 2002 FEBS 2002 Variations in receptor site-3 on rat brain and insect sodium channels highlighted by binding of a funnel-web spider d-atracotoxin Nicolas Gilles1 Greg Harrison1 Izhar Karbat2 Michael Gurevitz2 Graham M. Nicholson and Dalia Gordon2 1CEA Departement d Ingenierie et d Etudes des Proteines Gif-sur-Yvette France 2 Department of Plant Sciences Tel Aviv University Israel 3Department of Health Sciences University of Technology Sydney Australia S-Atracotoxins ỗ-ACTXs from Australian funnel-web spiders differ structurally from scorpion a-toxins ScaTx but similarly slow sodium current inactivation and compete for their binding to sodium channels at receptor site-3. Characterization of the binding of 125I-labelled S-ACTX-Hvla to various sodium channels reveals a decrease in affinity for depolarized 0 mV Kd nM -55mV Ki nM rat brain synaptosomes. The increased Kd under depolarized conditions correlates with a reduction in the association rate and a in the dissociation rate. In comparison ScaTx binding affinity decreased 33-fold under depolarized conditions due to a 48-fold reduction in the association rate. The binding of 125I-labelled Ỗ-ACTX-Hv1a to rat brain syna-ptosomes is inhibited competitively by classical ScaTxs and allosterically by brevetoxin-1 similar to ScaTx binding. However in contrast with classical ScaTxs 125I-labelled S-ACTX-Hv1a binds with high affinity to cockroach Na channels Ki nM and is displaced by the ScaTx LqhaIT a well-denned ligand of insect sodium channel receptor site-3. However S-ACTX-Hv1a exhibits a surprisingly low binding affinity to locust sodium channels. Thus unlike ScaTxs which are capable of differentiating between mammalian and insect sodium channels S-ACTXs differentiate between various insect sodium channels but bind with similar high affinity to rat brain and cockroach channels. Structural comparison of S-ACTX-Hv1a to ScaTxs .

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