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1tt3
From Proteopedia
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[[Image:1tt3.jpg|left|200px]] | [[Image:1tt3.jpg|left|200px]] | ||
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| - | + | {{STRUCTURE_1tt3| PDB=1tt3 | SCENE= }} | |
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'''NMR soulution structure of omega-conotoxin [K10]MVIIA''' | '''NMR soulution structure of omega-conotoxin [K10]MVIIA''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TT3 is a [[Single protein]] structure | + | 1TT3 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TT3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Smith, A B.]] | [[Category: Smith, A B.]] | ||
[[Category: Yasuda, T.]] | [[Category: Yasuda, T.]] | ||
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| - | [[Category: | + | [[Category: Four loop frame work]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:19:46 2008'' | |
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Revision as of 07:19, 3 May 2008
NMR soulution structure of omega-conotoxin [K10]MVIIA
Overview
Neurotransmitter release from preganglionic parasympathetic neurons is resistant to inhibition by selective antagonists of L-, N-, P/Q-, R-, and T-type calcium channels. In this study, the effects of different omega-conotoxins from genus Conus were investigated on current flow-through cloned voltage-sensitive calcium channels expressed in Xenopus oocytes and nerve-evoked transmitter release from the intact preganglionic cholinergic nerves innervating the rat submandibular ganglia. Our results indicate that omega-conotoxin CVID from Conus catus inhibits a pharmacologically distinct voltage-sensitive calcium channel involved in neurotransmitter release, whereas omega-conotoxin MVIIA had no effect. omega-Conotoxin CVID and MVIIA inhibited depolarization-activated Ba(2+) currents recorded from oocytes expressing N-type but not L- or R-type calcium channels. High affinity inhibition of the CVID-sensitive calcium channel was enhanced when position 10 of the omega-conotoxin was occupied by the smaller residue lysine as found in CVID instead of an arginine as found in MVIIA. Given that relatively small differences in the sequence of the N-type calcium channel alpha(1B) subunit can influence omega-conotoxin access (Feng, Z. P., Hamid, J., Doering, C., Bosey, G. M., Snutch, T. P., and Zamponi, G. W. (2001) J. Biol. Chem. 276, 15728-15735), it is likely that the calcium channel in preganglionic nerve terminals targeted by CVID is a N-type (Ca(v)2.2) calcium channel variant.
About this Structure
1TT3 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Omega-conotoxin CVID inhibits a pharmacologically distinct voltage-sensitive calcium channel associated with transmitter release from preganglionic nerve terminals., Adams DJ, Smith AB, Schroeder CI, Yasuda T, Lewis RJ, J Biol Chem. 2003 Feb 7;278(6):4057-62. Epub 2002 Nov 18. PMID:12441339 Page seeded by OCA on Sat May 3 10:19:46 2008
