Metal binding and conformational studies of the calcium binding domain of NADPH oxidase 5 reveal its similarity and difference to calmodulin.

Wei, Chin-Chuan; Fabry, Emily; Hay, Evan; Lloyd, Laura; Kaufman, Nichole; Yang, Ya-Ping; Stuehr, Dennis J

Wei, Chin-Chuan; Fabry, Emily; Hay, Evan; Lloyd, Laura; Kaufman, Nichole; Yang, Ya-Ping; Stuehr, Dennis J.

Afiliação

Wei CC; Department of Chemistry, Southern Illinois University Edwardsville, Edwardsville, Illinois, USA.
Fabry E; Department of Chemistry, Southern Illinois University Edwardsville, Edwardsville, Illinois, USA.
Hay E; Department of Chemistry, Southern Illinois University Edwardsville, Edwardsville, Illinois, USA.
Lloyd L; Department of Chemistry, Southern Illinois University Edwardsville, Edwardsville, Illinois, USA.
Kaufman N; Department of Chemistry, Southern Illinois University Edwardsville, Edwardsville, Illinois, USA.
Yang YP; Department of Pathobiology, the Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio, USA.
Stuehr DJ; Department of Pathobiology, the Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio, USA.

J Biomol Struct Dyn ; 38(8): 2352-2368, 2020 May.

Article em En | MEDLINE | ID: mdl-31203730

Assuntos

Calmodulina; NADPH Oxidase 5; Sítios de Ligação; Cálcio/metabolismo; Calmodulina/metabolismo; NADPH Oxidase 5/metabolismo; Ligação Proteica; Conformação Proteica

Palavras-chave

EF-hand; NADPH Oxidase 5; calcium binding; fluorescence; isothermal titration calorimetry

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Calmodulina / NADPH Oxidase 5 Tipo de estudo: Prognostic_studies Idioma: En Revista: J Biomol Struct Dyn Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Estados Unidos País de publicação: Reino Unido

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