1d1h

From Proteopedia

(Difference between revisions)

Revision as of 19:56, 25 December 2014

SOLUTION STRUCTURE OF HANATOXIN 1

Structural highlights

1d1h is a 1 chain structure with sequence from Grammostola rosea. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[TXHN1_GRASP] Inhibits Kv2.1/KCNB1 and Kv4.2/KCND2 voltage-gated potassium channels. Acts as a gating modifier by shifting channel openings to more depolarized voltages and acts via the occupancy of multiple binding sites on the channel. The toxin binding sites are situated on the S3-S4 extracellular linker of the channel. At least two hanatoxin molecules can occupy the Kv2.1/KCNB1 channel, and maybe more (three or four). Can also inhibit calcium channels (Cav2.1/CACNA1A). Needs to partition into the membrane in order to bind to the channel.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

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.

Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins.,Takahashi H, Kim JI, Min HJ, Sato K, Swartz KJ, Shimada I J Mol Biol. 2000 Mar 31;297(3):771-80. PMID:10731427^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Swartz KJ, MacKinnon R. Hanatoxin modifies the gating of a voltage-dependent K+ channel through multiple binding sites. Neuron. 1997 Apr;18(4):665-73. PMID:9136774
↑ Swartz KJ, MacKinnon R. Mapping the receptor site for hanatoxin, a gating modifier of voltage-dependent K+ channels. Neuron. 1997 Apr;18(4):675-82. PMID:9136775
↑ Li-Smerin Y, Swartz KJ. Gating modifier toxins reveal a conserved structural motif in voltage-gated Ca2+ and K+ channels. Proc Natl Acad Sci U S A. 1998 Jul 21;95(15):8585-9. PMID:9671721
↑ Herrington J. Gating modifier peptides as probes of pancreatic beta-cell physiology. Toxicon. 2007 Feb;49(2):231-8. Epub 2006 Sep 23. PMID:17101164 doi:http://dx.doi.org/S0041-0101(06)00354-0
↑ Takahashi H, Kim JI, Min HJ, Sato K, Swartz KJ, Shimada I. Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins. J Mol Biol. 2000 Mar 31;297(3):771-80. PMID:10731427 doi:http://dx.doi.org/10.1006/jmbi.2000.3609

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1d1h"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1d1h RCSB], [http://www.ebi.ac.uk/pdbsum/1d1h PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TXHN1_GRASP TXHN1_GRASP]] Inhibits Kv2.1/KCNB1 and Kv4.2/KCND2 voltage-gated potassium channels. Acts as a gating modifier by shifting channel openings to more depolarized voltages and acts via the occupancy of multiple binding sites on the channel. The toxin binding sites are situated on the S3-S4 extracellular linker of the channel. At least two hanatoxin molecules can occupy the Kv2.1/KCNB1 channel, and maybe more (three or four). Can also inhibit calcium channels (Cav2.1/CACNA1A). Needs to partition into the membrane in order to bind to the channel.<ref>PMID:9136774</ref> <ref>PMID:9136775</ref> <ref>PMID:9671721</ref> <ref>PMID:17101164</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

1d1h

From Proteopedia

Revision as of 19:56, 25 December 2014

SOLUTION STRUCTURE OF HANATOXIN 1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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