2kbh | pdb_00002kbh

solution structure of BmKalphaTx11 (major conformation)

spinqualitylabelsall models 2kbh, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kbh is a 1 chain structure with sequence from Mesobuthus martensii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2kbj, 2kbk Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SC11_MESMA] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission (By similarity). Shows analgesic activity when intraperitoneally injected into mice. 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 solution structure of BmKalphaTx11 presented by this paper is distinctive from any other structures of wide-type scorpion alpha-toxins reported so far, for its trans-9,10 peptide bond conformation is accompanied by 'protruding' topology of the 'NC-domain'. The orientation of the C-tail of BmKalphaTx11 is obviously different from that of classical alpha-toxins (e.g., AaH2, BmK-M8), despite the fact that they share common trans conformation of peptide bond between residues 9 and 10. Accordingly, there must be other structural factors dominating the orientation of the C-tail except the conformation of peptide bond 9-10. Our study reveals that residues at position 58 play an important role in it, and different type of residues at this position (e.g., Lys, Arg, Met, Ile) result in different spatial relationship between the C-terminus and the 'five-residue-turn' and then different topology of the 'NC-domain', therefore residues at position 58 are believed to function as structure and bioactivity switch for specificity of scorpion alpha-toxins. The mechanism for stabilizing the geometry of the 'NC-domain' in wide-type scorpion alpha-toxins is also discussed. Solution structure of BmKalphaTx11, a toxin from the venom of the Chinese scorpion Buthus martensii Karsch.,Zhu J, Tong X, Cao C, Wu G, Zhang N, Wu H Biochem Biophys Res Commun. 2010 Jan 1;391(1):627-33. Epub 2009 Nov 22. PMID:19932686 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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