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Title
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Structure and structure-function relationships of sea anemone proteins that interact with the sodium channel.
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Author
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R.S.Norton.
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Ref.
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Toxicon, 1991,
29,
1051-1084.
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PubMed id
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Abstract
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Sea anemones produce a series of toxic polypeptides and proteins with molecular
weights in the range 3000-5000 that act by binding to specific receptor sites on
the voltage-gated sodium channel of excitable tissue. This article reviews our
current knowledge of the molecular basis for activity of these molecules, with
particular emphasis on recent results on their receptor binding properties, the
role of individual residues in activity and receptor binding, and their
three-dimensional structures as determined by nuclear magnetic resonance
spectroscopy. A region of these molecules that constitutes at least part of the
receptor binding domain is proposed.
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