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PDBsum entry 1d1h

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Toxin PDB id
1d1h
Contents
Protein chain
35 a.a. *
* Residue conservation analysis

References listed in PDB file
Key reference
Title Solution structure of hanatoxin1, A gating modifier of voltage-Dependent k(+) channels: common surface features of gating modifier toxins.
Authors H.Takahashi, J.I.Kim, H.J.Min, K.Sato, K.J.Swartz, I.Shimada.
Ref. J Mol Biol, 2000, 297, 771-780. [DOI no: 10.1006/jmbi.2000.3609]
PubMed id 10731427
Abstract
The three-dimensional structure of hanatoxin1 (HaTx1) was determined by using NMR spectroscopy. HaTx1 is a 35 amino acid residue peptide toxin that inhibits the drk1 voltage-gated K(+) channel not by blocking the pore, but by altering the energetics of gating. Both the amino acid sequence of HaTx1 and its unique mechanism of action distinguish this toxin from the previously described K(+) channel inhibitors. Unlike most other K(+) channel-blocking toxins, HaTx1 adopts an "inhibitor cystine knot" motif and is composed of two beta-strands, strand I for residues 19-21 and strand II for residues 28-30, connected by four chain reversals. A comparison of the surface features of HaTx1 with those of other gating modifier toxins of voltage-gated Ca(2+) and Na(+) channels suggests that the combination of a hydrophobic patch and surrounding charged residues is principally responsible for the binding of gating modifier toxins to voltage-gated ion channels.
Figure 6.
Figure 6. (a) Surface profile of HaTx1. (b) Stereo view of the backbone and side-chain heavy atoms of HaTx1. In (a) and (b), hydrophobic residues (Ala, Cys, Ile, Leu, Met, Phe, Pro, Trp, Tyr and Val) are green; basic (Arg and Lys) and acidic (Asp and Glu) residues are blue and red, respectively. The residues in the surface hydrophobic patch and the surrounding charged residues are labeled.
Figure 7.
Figure 7. Comparison of surface profile between (a) CsE-V (PDB code 1NRA) and (b) ATX III (PDB code 1ANS). The color code is the same as that of Figure 6. The residues which belong to a hydrophobic patch and surrounding basic residues are labeled.
The above figures are reprinted by permission from Elsevier: J Mol Biol (2000, 297, 771-780) copyright 2000.
Secondary reference #1
Title An inhibitor of the kv2.1 potassium channel isolated from the venom of a chilean tarantula.
Authors K.J.Swartz, R.Mackinnon.
Ref. Neuron, 1995, 15, 941-949. [DOI no: 10.1016/0896-6273(95)90184-1]
PubMed id 7576642
Full text Abstract
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