1den | pdb_00001den

PROTEINASE INHIBITOR HOMOLOGUES AS POTASSIUM CHANNEL BLOCKERS

spinqualitylabelsall models 1den, 29 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1den is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1dem Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VKTH1_DENPO] Serine protease inhibitor homolog that blocks voltage-gated potassium channels (Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.6/KCNA6) (IC(50)=0.13-50 nM). 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 We report here the NMR structure of dendrotoxin I, a powerful potassium channel blocker from the venom of the African Elapidae snake Dendroaspis polylepis polylepis (black mamba), calculated from an experimentally-derived set of 719 geometric restraints. The backbone of the toxin superimposes on bovine pancreatic trypsin inhibitor (BPTI) with a root-mean-square deviation of < 1.7 A. The surface electrostatic potential calculated for dendrotoxin I and BPTI, reveal an important difference which might account for the differences in function of the two proteins. These proteins may provide examples of adaptation for specific and diverse biological functions while at the same time maintaining the overall three-dimensional structure of a common ancestor. Proteinase inhibitor homologues as potassium channel blockers.,Lancelin JM, Foray MF, Poncin M, Hollecker M, Marion D Nat Struct Biol. 1994 Apr;1(4):246-50. PMID:7544683 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dendrotoxin

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