The Startle Disease Mutation E103K Impairs Activation of Human Homomeric &#945;1 Glycine Receptors by Disrupting an Intersubunit Salt Bridge across the Agonist Binding Site.

Safar, Fatemah; Hurdiss, Elliot; Erotocritou, Marios; Greiner, Timo; Lape, Remigijus; Irvine, Mark W; Fang, Guangyu; Jane, David; Yu, Rilei; Dämgen, Marc A; Biggin, Philip C; Sivilotti, Lucia G

The Startle Disease Mutation E103K Impairs Activation of Human Homomeric α1 Glycine Receptors by Disrupting an Intersubunit Salt Bridge across the Agonist Binding Site.

Safar, Fatemah; Hurdiss, Elliot; Erotocritou, Marios; Greiner, Timo; Lape, Remigijus; Irvine, Mark W; Fang, Guangyu; Jane, David; Yu, Rilei; Dämgen, Marc A; Biggin, Philip C; Sivilotti, Lucia G.

Afiliação

Safar F; From the Department of Neuroscience, Physiology and Pharmacology, University College London, Gower Street, London WC1E 6BT, United Kingdom.
Hurdiss E; From the Department of Neuroscience, Physiology and Pharmacology, University College London, Gower Street, London WC1E 6BT, United Kingdom.
Erotocritou M; From the Department of Neuroscience, Physiology and Pharmacology, University College London, Gower Street, London WC1E 6BT, United Kingdom.
Greiner T; From the Department of Neuroscience, Physiology and Pharmacology, University College London, Gower Street, London WC1E 6BT, United Kingdom.
Lape R; From the Department of Neuroscience, Physiology and Pharmacology, University College London, Gower Street, London WC1E 6BT, United Kingdom.
Irvine MW; the School of Physiology and Pharmacology, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom, and.
Fang G; the School of Physiology and Pharmacology, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom, and.
Jane D; the School of Physiology and Pharmacology, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom, and.
Yu R; the Department of Biochemistry, Structural Bioinformatics and Computational Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.
Dämgen MA; the Key Laboratory of Marine Drugs, Chinese Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, China.
Biggin PC; the Department of Biochemistry, Structural Bioinformatics and Computational Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.
Sivilotti LG; the Department of Biochemistry, Structural Bioinformatics and Computational Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.

J Biol Chem ; 292(12): 5031-5042, 2017 03 24.

Article em En | MEDLINE | ID: mdl-28174298

Assuntos

Hiperecplexia/genética; Mutação Puntual; Receptores de Glicina/genética; Receptores de Glicina/metabolismo; Sequência de Aminoácidos; Cristalografia por Raios X; Glicina/metabolismo; Células HEK293; Humanos; Hiperecplexia/metabolismo; Modelos Moleculares; Mutagênese Sítio-Dirigida; Receptores de Glicina/química; Sarcosina/metabolismo; Alinhamento de Sequência

Palavras-chave

agonists; efficacy; glycine receptor; homology modeling; ion channel; mutagenesis; patch clamp; potency; site-directed mutagenesis

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Mutação Puntual / Receptores de Glicina / Hiperecplexia Limite: Humans Idioma: En Revista: J Biol Chem Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Reino Unido

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