1dtk

THE NMR SOLUTION STRUCTURE OF DENDROTOXIN K FROM THE VENOM OF DENDROASPIS POLYLEPIS POLYLEPISTHE NMR SOLUTION STRUCTURE OF DENDROTOXIN K FROM THE VENOM OF DENDROASPIS POLYLEPIS POLYLEPIS

Structural highlights

1dtk is a 1 chain structure with sequence from Dendroaspis polylepis polylepis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VKTHK_DENPO Serine protease inhibitor homolog that selectively blocks voltage-gated potassium channels homooligomer Kv1.1/KCNA1 (EC(50)=0.6 nM) and Kv1.1-containing heterooligomer.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Wang FC, Bell N, Reid P, Smith LA, McIntosh P, Robertson B, Dolly JO. Identification of residues in dendrotoxin K responsible for its discrimination between neuronal K+ channels containing Kv1.1 and 1.2 alpha subunits. Eur J Biochem. 1999 Jul;263(1):222-9. PMID:10429207
↑ Robertson B, Owen D, Stow J, Butler C, Newland C. Novel effects of dendrotoxin homologues on subtypes of mammalian Kv1 potassium channels expressed in Xenopus oocytes. FEBS Lett. 1996 Mar 25;383(1-2):26-30. PMID:8612784
↑ Owen DG, Hall A, Stephens G, Stow J, Robertson B. The relative potencies of dendrotoxins as blockers of the cloned voltage-gated K+ channel, mKv1.1 (MK-1), when stably expressed in Chinese hamster ovary cells. Br J Pharmacol. 1997 Mar;120(6):1029-34. PMID:9134213 doi:http://dx.doi.org/10.1038/sj.bjp.0701004

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OCA

[1] Wang FC, Bell N, Reid P, Smith LA, McIntosh P, Robertson B, Dolly JO. Identification of residues in dendrotoxin K responsible for its discrimination between neuronal K+ channels containing Kv1.1 and 1.2 alpha subunits. Eur J Biochem. 1999 Jul;263(1):222-9. PMID:10429207

[2] Robertson B, Owen D, Stow J, Butler C, Newland C. Novel effects of dendrotoxin homologues on subtypes of mammalian Kv1 potassium channels expressed in Xenopus oocytes. FEBS Lett. 1996 Mar 25;383(1-2):26-30. PMID:8612784

[3] Owen DG, Hall A, Stephens G, Stow J, Robertson B. The relative potencies of dendrotoxins as blockers of the cloned voltage-gated K+ channel, mKv1.1 (MK-1), when stably expressed in Chinese hamster ovary cells. Br J Pharmacol. 1997 Mar;120(6):1029-34. PMID:9134213 doi:http://dx.doi.org/10.1038/sj.bjp.0701004

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