Cargando…
The active site region plays a critical role in Na(+) binding to thrombin
The catalytic activity of thrombin and other enzymes of the blood coagulation and complement cascades is enhanced significantly by binding of Na(+) to a site >15 Å away from the catalytic residue S195, buried within the 180 and 220 loops that also contribute to the primary specificity of the enzy...
Autores principales: | Pelc, Leslie A., Koester, Sarah K., Kukla, Cassandra R., Chen, Zhiwei, Di Cera, Enrico |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8695361/ https://www.ncbi.nlm.nih.gov/pubmed/34861239 http://dx.doi.org/10.1016/j.jbc.2021.101458 |
Ejemplares similares
-
Residues W215, E217 and E192 control the allosteric E*-E equilibrium of thrombin
por: Pelc, Leslie A., et al.
Publicado: (2019) -
Role of the I16-D194 ionic interaction in the trypsin fold
por: Stojanovski, Bosko M., et al.
Publicado: (2019) -
(19)F NMR reveals the conformational properties of free thrombin and its zymogen precursor prethrombin-2
por: Ruben, Eliza A., et al.
Publicado: (2020) -
Role of the activation peptide in the mechanism of protein C activation
por: Stojanovski, Bosko M., et al.
Publicado: (2020) -
Probing prothrombin structure by limited proteolysis
por: Acquasaliente, Laura, et al.
Publicado: (2019)