Cargando…
Conformational preference of ChaK1 binding peptides: a molecular dynamics study
TRPM7/ChaK1 is a recently discovered atypical protein kinase that has been suggested to selectively phosphorylate the substrate residues located in α-helices. However, the actual structure of kinase-substrate complex has not been determined experimentally and the recognition mechanism remains unknow...
Autores principales: | Zhang, Jiajing, King, Christopher A, Dalby, Kevin, Ren, Pengyu |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2831825/ https://www.ncbi.nlm.nih.gov/pubmed/20180991 http://dx.doi.org/10.1186/1757-5036-3-2 |
Ejemplares similares
-
Establishing communication mechanism for malaria prevention in Baiga tribal villages in Baiga Chak area of Dindori district, Madhya Pradesh
por: Saha, Kalyan B., et al.
Publicado: (2015) -
Using docking and alchemical free energy approach to determine the binding mechanism of eEF2K inhibitors and prioritizing the compound synthesis
por: Wang, Qiantao, et al.
Publicado: (2015) -
Conformational Preferences of Pyridone Adenine Dinucleotides from Molecular Dynamics Simulations
por: Buckley, David P., et al.
Publicado: (2022) -
A Model of a MAPK•Substrate Complex in an Active Conformation: A Computational and Experimental Approach
por: Lee, Sunbae, et al.
Publicado: (2011) -
Characterizing the conformational landscape of MDM2-binding p53 peptides using Molecular Dynamics simulations
por: Yadahalli, Shilpa, et al.
Publicado: (2017)