1lmr

Solution of ADO1, a Toxin from the Assassin Bugs Agriosphodrus dohrni that Blocks the Voltage Sensitive Calcium Channel L-type

spinqualitylabelsall models 1lmr, 21 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lmr is a 1 chain structure with sequence from Agrdo. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ADO1_AGRDO] Binds reversibly and blocks P/Q-type voltage-gated calcium channels (Cav). Publication Abstract from PubMed ADO1 is a toxin purified from the saliva of the assassin bug, Agriosphodrus dohrni. Because of its similarity in sequence to Ptu1 from another assassin bug, we did not assess its pharmacologic target. Here, we demonstrate by electrophysiologic means that ADO1 targets the P/Q-type voltage-sensitive calcium channel. We also determine the solution structure of ADO1 using two-dimensional NMR techniques, followed by distance geometry and molecular dynamics. The structure of ADO1 belongs to the inhibitory cystine knot (ICK) structural family (i.e., a compact disulfide-bonded core from which four loops emerge). ADO1 contains a two-stranded, antiparallel beta-sheet structure. We compare the structure of ADO1 with other voltage-sensitive calcium-channel blockers, analyze the topologic juxtaposition of key functional residues, and conclude that the recognition of voltage-sensitive calcium channels by toxins belonging to the ICK structural family requires residues located on two distinct areas of the molecular surface of the toxins. Solution structure of ADO1, a toxin extracted from the saliva of the assassin bug, Agriosphodrus dohrni.,Bernard C, Corzo G, Adachi-Akahane S, Foures G, Kanemaru K, Furukawa Y, Nakajima T, Darbon H Proteins. 2004 Feb 1;54(2):195-205. PMID:14696181 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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