1y29: Difference between revisions
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[[Image:1y29.gif|left|200px]] | [[Image:1y29.gif|left|200px]] | ||
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{{STRUCTURE_1y29| PDB=1y29 | SCENE= }} | |||
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'''Three dimensional solution structure of huwentoxin-x by 2D 1H-NMR''' | '''Three dimensional solution structure of huwentoxin-x by 2D 1H-NMR''' | ||
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==About this Structure== | ==About this Structure== | ||
1Y29 is a [[Single protein]] structure | 1Y29 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y29 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Liang, S.]] | [[Category: Liang, S.]] | ||
[[Category: Liu, Z.]] | [[Category: Liu, Z.]] | ||
[[Category: | [[Category: A double-stranded beta-sheet]] | ||
[[Category: | [[Category: Ick]] | ||
[[Category: | [[Category: Knottin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:47:48 2008'' | |||
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Revision as of 12:47, 3 May 2008
Three dimensional solution structure of huwentoxin-x by 2D 1H-NMR
Overview
Huwentoxin-X (HWTX-X) is a novel peptide toxin, purified from the venom of the spider Ornithoctonus huwena. It comprises 28 amino acid residues including six cysteine residues as disulfide bridges linked in the pattern of I-IV, II-V, and III-VI. Its cDNA, determined by rapid amplification of 3' and 5' cDNA ends, encodes a 65-residue prepropeptide. HWTX-X shares low sequence homology with omega-conotoxins GVIA and MVIIA, two well known blockers of N-type Ca2+ channels. Nevertheless, whole cell studies indicate that it can block N-type Ca2+ channels in rat dorsal root ganglion cells (IC50 40 nm) and the blockage by HWTX-X is completely reversible. The rank order of specificity for N-type Ca2+ channels is GVIA approximately HWTX-X > MVIIA. In contrast to GVIA and MVIIA, HWTX-X had no detectable effect on the twitch response of rat vas deferens to low frequency electrical stimulation, indicating that HWTX-X has different selectivity for isoforms of N-type Ca2+ channels, compared with GVIA or MVIIA. A comparison of the structures of HWTX-X and GVIA reveals that they not only adopt a common structural motif (inhibitor cystine knot), but also have a similar functional motif, a binding surface formed by the critical residue Tyr, and several basic residues. However, the dissimilarities of their binding surfaces provide some insights into their different selectivities for isoforms of N-type Ca2+ channels.
About this Structure
1Y29 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Function and solution structure of Huwentoxin-X, a specific blocker of N-type calcium channels, from the Chinese bird spider Ornithoctonus huwena., Liu Z, Dai J, Dai L, Deng M, Hu Z, Hu W, Liang S, J Biol Chem. 2006 Mar 31;281(13):8628-35. Epub 2006 Jan 26. PMID:16439354 Page seeded by OCA on Sat May 3 15:47:48 2008
