Specificity and affinity of the N-terminal residues in staphylocoagulase in binding to prothrombin.

Maddur, Ashoka A; Kroh, Heather K; Aschenbrenner, Mary E; Gibson, Breanne H Y; Panizzi, Peter; Sheehan, Jonathan H; Meiler, Jens; Bock, Paul E; Verhamme, Ingrid M

Maddur, Ashoka A; Kroh, Heather K; Aschenbrenner, Mary E; Gibson, Breanne H Y; Panizzi, Peter; Sheehan, Jonathan H; Meiler, Jens; Bock, Paul E; Verhamme, Ingrid M.

Afiliação

Maddur AA; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee 37232-2561. Electronic address: ashoka.maddur@vumc.org.
Kroh HK; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee 37232-2561.
Aschenbrenner ME; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee 37232-2561.
Gibson BHY; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee 37232-2561.
Panizzi P; Department of Drug Discovery and Development, Harrison School of Pharmacy, Auburn University, Auburn, Alabama 36849.
Sheehan JH; Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232.
Meiler J; Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232; Institute for Drug Discovery, Departments of Chemistry and Computer Science, Leipzig University Medical School, SAC 04103 Leipzig, Germany.
Bock PE; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee 37232-2561.
Verhamme IM; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee 37232-2561. Electronic address: ingrid.verhamme@vanderbilt.edu.

J Biol Chem ; 295(17): 5614-5625, 2020 04 24.

Article em En | MEDLINE | ID: mdl-32156702

Assuntos

Proteínas de Bactérias/metabolismo; Coagulase/metabolismo; Protrombina/metabolismo; Staphylococcus aureus/metabolismo; Proteínas de Bactérias/química; Sítios de Ligação; Coagulase/química; Humanos; Modelos Moleculares; Ligação Proteica; Protrombina/química; Infecções Estafilocócicas/metabolismo; Infecções Estafilocócicas/microbiologia; Staphylococcus aureus/química; Especificidade por Substrato

Palavras-chave

Staphylococcus aureus (S. aureus); affinity; clot formation; coagulation; coagulation factor; competitive equilibrium binding; endocarditis; equilibrium binding; fibrin; kinetics; ligand-binding protein; prothrombin; specificity; staphylocoagulase (SC); virulence factor

Texto completo

Adicionar na Minha BVS

Imprimir

XML

PubMed Links

Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Staphylococcus aureus / Proteínas de Bactérias / Protrombina / Coagulase Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Revista: J Biol Chem Ano de publicação: 2020 Tipo de documento: Article País de publicação: Estados Unidos

Texto completo

Adicionar na Minha BVS

Imprimir

XML

PubMed Links

Buscar no Google