1D1H

SOLUTION STRUCTURE OF HANATOXIN 1

Summary for 1D1H

• Entry DOI: 10.2210/pdb1d1h/pdb
• Descriptor: HANATOXIN TYPE 1 (1 entity in total)
• Functional Keywords: cystine knot, toxin
• Biological source: Grammostola rosea
• Cellular location: Secreted: P56852
• Total number of polymer chains: 1
• Total formula weight: 4127.77

Authors

Takahashi, H.,Kim, J.I.,Sato, K.,Swartz, K.J.,Shimada, I. (deposition date: 1999-09-16, release date: 2000-09-20, Last modification date: 2024-10-30)

Primary citation

Takahashi, H.,Kim, J.I.,Min, H.J.,Sato, K.,Swartz, K.J.,Shimada, I.
Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins.
J.Mol.Biol., 297:771-780, 2000

PubMed 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.

PubMed: 10731427
DOI: 10.1006/jmbi.2000.3609

Experimental method

SOLUTION NMR