Deciphering the Arginine-binding preferences at the substrate-binding groove of Ser/Thr kinases by computational surface mapping.
Protein kinases are key signaling enzymes that catalyze the transfer of γ-phosphate from an ATP molecule to a phospho-accepting residue in the substrate. Unraveling the molecular features that govern the preference of kinases for particular residues flanking the phosphoacceptor is important for unde...
Main Authors: | Avraham Ben-Shimon, Masha Y Niv |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2011-11-01
|
Series: | PLoS Computational Biology |
Online Access: | http://europepmc.org/articles/PMC3219626?pdf=render |
Similar Items
-
Substrate Specificity of Recombinant Ser/Thr Protein Kinase
by: Anna Zorina, et al.
Published: (2015-03-01) -
Primate-specific isoform of Nedd4-1 regulates substrate binding via Ser/Thr phosphorylation and 14-3-3 binding
by: George Kefalas, et al.
Published: (2023-10-01) -
A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases.
by: Fedorov, O, et al.
Published: (2007) -
The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization.
by: Mushtaq Mir, et al.
Published: (2011-07-01) -
Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes
by: Krupa A, et al.
Published: (2005-09-01)