1ctx | pdb_00001ctx

THREE-DIMENSIONAL STRUCTURE OF THE-LONG-NEUROTOXIN FROM COBRA VENOM

spinqualitylabelsall models 1ctx, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ctx is a 1 chain structure with sequence from Naja siamensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [NXL1_NAJKA] The monomeric form binds with high affinity to muscular, Torpedo (muscle-type), and neuronal alpha-7 nicotinic acetylcholine receptors (nAChR). Has no effect on alpha-3/beta-2 nAChR. Causes paralysis by preventing acetylcholine binding to the nAChR. Does not show any blockade of the nicotine-evoked release of dopamine and does not affect ACh release. In mice lung cancer, causes reduction of tumor growth. The homodimeric form binds with low affinity to Torpedo (muscle-type) and alpha-7 nAChRs, whereas it acquires the capacity to block alpha-3/beta-2 nAChRs. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The three-dimensional structure of alpha-cobra-toxin, the "long" neurotoxin from the venom of Naja naja siamensis, has been determined at 2.8-A resolution. Crystals grown as hexagonal needles have space group P6522 with unit cell parameters a = b = 74.59 A, c = 42.89 A; one molecule per asymmetric unit. Phases were determined with a single isomorphous derivative with HgI2 by using the anomalous scattering of the single-site HgI2 molecule to resolve the phase ambiguity. The polypeptide chain folds into three major loops and one tail emerging from a globular head. The protruding long central loop (residues 21-40) is flanked on either side by two shorter loops (residues 4-13 and 44-55); the tail piece (residues 63-71) hangs behind this loop. The molecular conformation is determined by four disulfides in the head and one at the tip of the long loop, by a triple-stranded beta-pleated sheet involving this loop, and by hydrophobic interactions stabilizing the other two loops. The structure of alpha-cobratoxin is compared to that described for the "short" erabutoxin b which shows similar arrangement of structurally and functionally invariant groups. Three-dimensional structure of the "long" neurotoxin from cobra venom.,Walkinshaw MD, Saenger W, Maelicke A Proc Natl Acad Sci U S A. 1980 May;77(5):2400-4. PMID:6930640 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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