Solution structure and functional investigation of human guanylate kinase reveals allosteric networking and a crucial role for the enzyme in cancer.

Khan, Nazimuddin; Shah, Parag P; Ban, David; Trigo-Mouriño, Pablo; Carneiro, Marta G; DeLeeuw, Lynn; Dean, William L; Trent, John O; Beverly, Levi J; Konrad, Manfred; Lee, Donghan; Sabo, T Michael

Khan, Nazimuddin; Shah, Parag P; Ban, David; Trigo-Mouriño, Pablo; Carneiro, Marta G; DeLeeuw, Lynn; Dean, William L; Trent, John O; Beverly, Levi J; Konrad, Manfred; Lee, Donghan; Sabo, T Michael.

Afiliação

Khan N; Department of Medicine, James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40202.
Shah PP; Department of Medicine, James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40202.
Ban D; Department of Medicine, James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40202.
Trigo-Mouriño P; Department for NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Carneiro MG; Department for NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
DeLeeuw L; Department of Medicine, James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40202.
Dean WL; Department of Medicine, James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40202.
Trent JO; Department of Medicine, James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40202.
Beverly LJ; Department of Medicine, James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40202.
Konrad M; Enzyme Biochemistry Group, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany mkonrad@mpibpc.mpg.de.
Lee D; Department of Medicine, James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40202 donghan.lee@louisville.edu.
Sabo TM; Department of Medicine, James Graham Brown Cancer Center, University of Louisville, Louisville, Kentucky 40202 mike.sabo@louisville.edu.

J Biol Chem ; 294(31): 11920-11933, 2019 08 02.

Article em En | MEDLINE | ID: mdl-31201273

Assuntos

Guanilato Quinases/metabolismo; Regulação Alostérica; Animais; Linhagem Celular Tumoral; Cristalografia por Raios X; Guanilato Quinases/química; Guanilato Quinases/genética; Humanos; Cinética; Neoplasias Pulmonares/metabolismo; Neoplasias Pulmonares/patologia; Camundongos; Mutagênese Sítio-Dirigida; Ressonância Magnética Nuclear Biomolecular; Estrutura Terciária de Proteína; Interferência de RNA; RNA Interferente Pequeno; Proteínas Recombinantes/biossíntese; Proteínas Recombinantes/química; Proteínas Recombinantes/isolamento & purificação

Palavras-chave

enzyme kinetics; enzyme mutation; guanylate kinase; hGMPK; lung cancer; non-synonymous single nucleotide variants (nsSNV); nuclear magnetic resonance (NMR); protein structure; solution structure

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Guanilato Quinases Idioma: En Ano de publicação: 2019 Tipo de documento: Article

Texto completo

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Guanilato Quinases Idioma: En Ano de publicação: 2019 Tipo de documento: Article