2lo7 | pdb_00002lo7

Ts16 NMR solution structure

spinqualitylabelsall models 2lo7, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lo7 is a 1 chain structure with sequence from Brazilian scorpion. This structure supersedes the now removed PDB entry 2lka. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Function [TTX16_TITSE] Blocks potassium channels (By similarity).[UniProtKB:P0C183] Publication Abstract from PubMed Scorpion venoms are a rich source of K(+) channel-blocking peptides. For the most part, they are structurally related small disulfide-rich proteins containing a conserved pattern of six cysteines that is assumed to dictate their common three-dimensional folding. In the conventional pattern, two disulfide bridges connect an alpha-helical segment to the C-terminal strand of a double- or triple-stranded beta-sheet, conforming a cystine-stabilized alpha/beta scaffold (CSalpha/beta). Here we show that two K(+) channel-blocking peptides from Tityus scorpions conserve the cysteine spacing of common scorpion venom peptides but display an unconventional disulfide pattern, accompanied by a complete rearrangement of the secondary structure topology into a CS helix-loop-helix fold. Sequence and structural comparisons of the peptides adopting this novel fold suggest that it would be a new elaboration of the widespread CSalpha/beta scaffold, thus revealing an unexpected structural versatility of these small disulfide-rich proteins. Acknowledgment of such versatility is important to understand how venom structural complexity emerged on a limited number of molecular scaffolds. New Tricks of an Old Pattern: STRUCTURAL VERSATILITY OF SCORPION TOXINS WITH COMMON CYSTEINE SPACING.,Saucedo AL, Flores-Solis D, Rodriguez de la Vega RC, Ramirez-Cordero B, Hernandez-Lopez R, Cano-Sanchez P, Navarro RN, Garcia-Valdes J, Coronas-Valderrama F, de Roodt A, Brieba LG, Possani LD, Del Rio-Portilla F J Biol Chem. 2012 Apr 6;287(15):12321-30. Epub 2012 Jan 10. PMID:22238341 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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