Unnatural amino acid mutagenesis of the GABA(A) receptor binding site residues reveals a novel cation-pi interaction between GABA and beta 2Tyr97 (Q37112916)

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scientific article published on January 2007

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English	Unnatural amino acid mutagenesis of the GABA(A) receptor binding site residues reveals a novel cation-pi interaction between GABA and beta 2Tyr97	scientific article published on January 2007

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24 December 2019

Unnatural amino acid mutagenesis of the GABA(A) receptor binding site residues reveals a novel cation-pi interaction between GABA and beta 2Tyr97 (English)

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24 December 2019

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24 December 2019

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Sarah C R Lummis

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24 December 2019

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Claire L Padgett

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24 December 2019

Ariele P Hanek

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24 December 2019

Dennis A Dougherty

4

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1 January 2007

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24 December 2019

Journal of Neuroscience

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24 December 2019

27

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24 December 2019

4

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24 December 2019

886-892

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24 December 2019

On the accuracy of homology modeling and sequence alignment methods applied to membrane proteins

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From ab initio quantum mechanics to molecular neurobiology: a cation-pi binding site in the nicotinic receptor

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An arginine involved in GABA binding and unbinding but not gating of the GABA(A) receptor.

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Defining the roles of Asn-128, Glu-129 and Phe-130 in loop A of the 5-HT3 receptor

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GABA(A) receptor beta 2 Tyr97 and Leu99 line the GABA-binding site. Insights into mechanisms of agonist and antagonist actions

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Structural and electrostatic properties of the 5-HT3 receptor pore revealed by substituted cysteine accessibility mutagenesis.

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In vivo incorporation of unnatural amino acids into ion channels in Xenopus oocyte expression system.

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Identifiers

10.1523/JNEUROSCI.4791-06.2007

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24 December 2019

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24 December 2019

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24 December 2019

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