Structure and structure-function relationships of sea anemone proteins that interact with the sodium channel.
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.
School of Biochemistry, University of New South Wales, Kensington, Australia.
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Norton
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003064:Cnidarian Venoms / Q000737:chemistry / Q000378:metabolism / Q000633:toxicity*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000378:metabolism / Q000633:toxicity*; D012615:Sea Anemones / Q000378:metabolism*; D015222:Sodium Channels / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D013329:Structure-Activity Relationship
D003064:Cnidarian Venoms; D011506:Proteins; D015222:Sodium Channels