1ux2: Difference between revisions
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[[Image:1ux2.gif|left|200px]]<br /> | [[Image:1ux2.gif|left|200px]]<br /><applet load="1ux2" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1ux2" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1ux2, resolution 2.2Å" /> | caption="1ux2, resolution 2.2Å" /> | ||
'''X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP)'''<br /> | '''X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1UX2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lymnaea_stagnalis Lymnaea stagnalis] with NAG, SO4, NH4 and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. | 1UX2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lymnaea_stagnalis Lymnaea stagnalis] with NAG, SO4, NH4 and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Nag Binding Site For Chain J'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UX2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: pentamer]] | [[Category: pentamer]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:15:38 2007'' | ||
Revision as of 19:05, 18 December 2007
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X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP)
OverviewOverview
Nicotinic acetylcholine receptors are prototypes for the pharmaceutically, important family of pentameric ligand-gated ion channels. Here we present, atomic resolution structures of nicotine and carbamylcholine binding to, AChBP, a water-soluble homolog of the ligand binding domain of nicotinic, receptors and their family members, GABAA, GABAC, 5HT3 serotonin, and, glycine receptors. Ligand binding is driven by enthalpy and is accompanied, by conformational changes in the ligand binding site. Residues in the, binding site contract around the ligand, with the largest movement in the, C loop. As expected, the binding is characterized by substantial aromatic, and hydrophobic contributions, but additionally there are close contacts, between protein oxygens and positively charged groups in the ligands. The, higher affinity of nicotine is due to a main chain hydrogen bond with the, B loop and a closer packing of the aromatic groups. These structures will, be useful tools for the development of new drugs involving nicotinic, acetylcholine receptor-associated diseases.
About this StructureAbout this Structure
1UX2 is a Single protein structure of sequence from Lymnaea stagnalis with NAG, SO4, NH4 and EPE as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures., Celie PH, van Rossum-Fikkert SE, van Dijk WJ, Brejc K, Smit AB, Sixma TK, Neuron. 2004 Mar 25;41(6):907-14. PMID:15046723
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