Cargando…
Side Chain Conformational Averaging in Human Dihydrofolate Reductase
[Image: see text] The three-dimensional structures of the dihydrofolate reductase enzymes from Escherichia coli (ecDHFR or ecE) and Homo sapiens (hDHFR or hE) are very similar, despite a rather low level of sequence identity. Whereas the active site loops of ecDHFR undergo major conformational rearr...
Autores principales: | Tuttle, Lisa M., Dyson, H. Jane, Wright, Peter E. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985697/ https://www.ncbi.nlm.nih.gov/pubmed/24498949 http://dx.doi.org/10.1021/bi4015314 |
Ejemplares similares
-
Divergent evolution of protein conformational dynamics in dihydrofolate reductase
por: Bhabha, Gira, et al.
Publicado: (2013) -
Cofactor-Mediated
Conformational Dynamics Promote
Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway
por: Oyen, David, et al.
Publicado: (2015) -
Tales of Dihydrofolate Binding to R67 Dihydrofolate
Reductase
por: Duff, Michael R., et al.
Publicado: (2015) -
Defining
the Structural Basis for Allosteric Product
Release from E. coli Dihydrofolate
Reductase Using NMR Relaxation Dispersion
por: Oyen, David, et al.
Publicado: (2017) -
Adaptations for Pressure and Temperature in Dihydrofolate Reductases
por: Penhallurick, Ryan W., et al.
Publicado: (2021)