1ien
From Proteopedia
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[[Image:1ien.gif|left|200px]] | [[Image:1ien.gif|left|200px]] | ||
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'''SOLUTION STRUCTURE OF TIA''' | '''SOLUTION STRUCTURE OF TIA''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IEN is a [[Single protein]] structure | + | 1IEN is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Sharpe, I A.]] | [[Category: Sharpe, I A.]] | ||
[[Category: Thomas, L.]] | [[Category: Thomas, L.]] | ||
| - | [[Category: | + | [[Category: Alpha1-adrenoceptor]] |
| - | [[Category: | + | [[Category: Conotoxin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:55:06 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:55, 2 May 2008
SOLUTION STRUCTURE OF TIA
Overview
Cone snails use venom containing a cocktail of peptides ('conopeptides') to capture their prey. Many of these peptides also target mammalian receptors, often with exquisite selectivity. Here we report the discovery of two new classes of conopeptides. One class targets alpha1-adrenoceptors (rho-TIA from the fish-hunting Conus tulipa), and the second class targets the neuronal noradrenaline transporter (chi-MrIA and chi-MrIB from the mollusk-hunting C. marmoreus). rho-TIA and chi-MrIA selectively modulate these important membrane-bound proteins. Both peptides act as reversible non-competitive inhibitors and provide alternative avenues for the identification of inhibitor drugs.
About this Structure
1IEN is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Two new classes of conopeptides inhibit the alpha1-adrenoceptor and noradrenaline transporter., Sharpe IA, Gehrmann J, Loughnan ML, Thomas L, Adams DA, Atkins A, Palant E, Craik DJ, Adams DJ, Alewood PF, Lewis RJ, Nat Neurosci. 2001 Sep;4(9):902-7. PMID:11528421 Page seeded by OCA on Fri May 2 19:55:06 2008
