1ien
From Proteopedia
SOLUTION STRUCTURE OF TIA
Structural highlights
Function[CA1A_CONTU] Allosteric inhibitor of alpha-1B adrenergic receptors (ADRA1B). Binds to an allosteric modulatory site on transmembrane helix 6 and 7 at the base of extracellular loop 3 of ADRA1B (PubMed:23184947). Also weekly inhibits alpha-1A (ADRA1A) and alpha-1D (ADRA1D) adrenergic receptors in a competive manner (PubMed:15194691). Potently inhibits contractions of vas deferens, spleen and aorta in response to noradrenaline (PubMed:15680270).[1] [2] [3] [4] [5] Publication Abstract from PubMedCone 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. 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[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Adams, D A | Adams, D J | Alewood, P F | Atkins, A | Craik, D J | Gehrmann, J | Lewis, R J | Loughnan, M L | Palant, E | Sharpe, I A | Thomas, L | Alpha1-adrenoceptor | Conotoxin | Toxin
