1koz

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Revision as of 08:44, 25 December 2014

SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA

Structural highlights

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

Function

[WGRTX_GRASP] Inhibits P/Q- (Cav2.1/CACNA1A) and N-type (Cav2.2/CACNA1B) voltage-gated calcium channel by modifying voltage-dependent gating. It selectively and reversibly blocks the calcium channels coupled to glutamate release. Also inhibits potassium channels (Kv2.1/KCNB1) with lower affinity.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

omega-Grammotoxin SIA (GrTx) is a 36 amino acid residue protein toxin from spider venom that inhibits P/Q and N-type voltage-gated Ca(2+) channels by modifying voltage-dependent gating. We determined the three-dimensional structure of GrTx using NMR spectroscopy. The toxin adopts an "inhibitor cystine knot" motif composed of two beta-strands (Leu19-Cys21 and Cys30-Trp32) and a beta-bulge (Trp6, Gly7-Cys30) with a +2x, -1 topology, which are connected by four chain reversals. Although GrTx was originally identified as an inhibitor of voltage-gated Ca(2+) channel, it also binds to K(+) channels with lower affinity. A similar cross-reaction was observed for Hanatoxin1 (HaTx), which binds to the voltage-sensing domains of K(+) and Ca(2+) channels with different affinities. A detailed comparison of the GrTx and HaTx structures identifies a conserved face containing a large hydrophobic patch surrounded by positively charged residues. The slight differences in the surface shape, which result from the orientation of the surface aromatic residues and/or the distribution of the charged residues, may explain the differences in the binding affinity of these gating modifiers with different voltage-gated ion channels.

Solution structure of omega-grammotoxin SIA, a gating modifier of P/Q and N-type Ca(2+) channel.,Takeuchi K, Park E, Lee C, Kim J, Takahashi H, Swartz K, Shimada I J Mol Biol. 2002 Aug 16;321(3):517-26. PMID:12162963^[6]

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

References

↑ Ono S, Kimura T, Kubo T. Characterization of voltage-dependent calcium channel blocking peptides from the venom of the tarantula Grammostola rosea. Toxicon. 2011 Sep 1;58(3):265-76. doi: 10.1016/j.toxicon.2011.06.006. Epub 2011, Jun 28. PMID:21740921 doi:http://dx.doi.org/10.1016/j.toxicon.2011.06.006
↑ Lampe RA, Defeo PA, Davison MD, Young J, Herman JL, Spreen RC, Horn MB, Mangano TJ, Keith RA. Isolation and pharmacological characterization of omega-grammotoxin SIA, a novel peptide inhibitor of neuronal voltage-sensitive calcium channel responses. Mol Pharmacol. 1993 Aug;44(2):451-60. PMID:8394998
↑ Piser TM, Lampe RA, Keith RA, Thayer SA. Complete and reversible block by omega-grammotoxin SIA of glutamatergic synaptic transmission between cultured rat hippocampal neurons. Neurosci Lett. 1995 Dec 8;201(2):135-8. PMID:8848236
↑ McDonough SI, Lampe RA, Keith RA, Bean BP. Voltage-dependent inhibition of N- and P-type calcium channels by the peptide toxin omega-grammotoxin-SIA. Mol Pharmacol. 1997 Dec;52(6):1095-104. PMID:9415720
↑ 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
↑ Takeuchi K, Park E, Lee C, Kim J, Takahashi H, Swartz K, Shimada I. Solution structure of omega-grammotoxin SIA, a gating modifier of P/Q and N-type Ca(2+) channel. J Mol Biol. 2002 Aug 16;321(3):517-26. PMID:12162963

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/1koz"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1koz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KOZ FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1koz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1koz RCSB], [http://www.ebi.ac.uk/pdbsum/1koz PDBsum]</span></td></tr>
+</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=1koz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1koz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1koz RCSB], [http://www.ebi.ac.uk/pdbsum/1koz PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/WGRTX_GRASP WGRTX_GRASP]] Inhibits P/Q- (Cav2.1/CACNA1A) and N-type (Cav2.2/CACNA1B) voltage-gated calcium channel by modifying voltage-dependent gating. It selectively and reversibly blocks the calcium channels coupled to glutamate release. Also inhibits potassium channels (Kv2.1/KCNB1) with lower affinity.<ref>PMID:21740921</ref> <ref>PMID:8394998</ref> <ref>PMID:8848236</ref> <ref>PMID:9415720</ref> <ref>PMID:9671721</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 19: @@
 __TOC__
 </StructureSection>
-[[Category: Kim, J I.]]
+[[Category: Kim, J I]]
-[[Category: Lee, C W.]]
+[[Category: Lee, C W]]
-[[Category: Park, E J.]]
+[[Category: Park, E J]]
-[[Category: Shimada, I.]]
+[[Category: Shimada, I]]
-[[Category: Swartz, K J.]]
+[[Category: Swartz, K J]]
-[[Category: Takahashi, H.]]
+[[Category: Takahashi, H]]
-[[Category: Takeuchi, K.]]
+[[Category: Takeuchi, K]]
 [[Category: Cystine knot]]
 [[Category: Toxin]]

1koz

From Proteopedia

Revision as of 08:44, 25 December 2014

SOLUTION STRUCTURE OF OMEGA-GRAMMOTOXIN SIA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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