Linear motif atlas for phosphorylation-dependent signaling.
|Abstract||Systematic and quantitative analysis of protein phosphorylation is revealing dynamic regulatory networks underlying cellular responses to environmental cues. However, matching these sites to the kinases that phosphorylate them and the phosphorylation-dependent binding domains that may subsequently bind to them remains a challenge. NetPhorest is an atlas of consensus sequence motifs that covers 179 kinases and 104 phosphorylation-dependent binding ... [truncated at 450 characters in length]|
|Author||Miller, Martin Lee; Jensen, Lars Juhl; Diella, Francesca; et al|
|Subject||14-3-3 Proteins Amino Acid Motifs Animals BRCA1 Protein Consensus Sequence Databases, Protein Humans Phosphorylation Phosphotransferases Phosphotyrosine Protein Binding Signal Transduction src Homology Domains chemistry chemistry chemistry metabolism|
Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site.
|Abstract||About 10% of all protein kinases are predicted to be enzymatically inactive pseudokinases, but the structural details of kinase inactivation have remained unclear. We present the first structure of a pseudokinase, VRK3, and that of its closest active relative, VRK2. Profound changes to the active site region underlie the loss of catalytic activity, and VRK3 cannot bind ATP because of residue substitutions in the binding pocket. However, VRK3 stil ... [truncated at 450 characters in length]|
|Author||Scheeff, Eric D; Eswaran, Jeyanthy; Bunkoczi, Gabor; et al|
|Subject||Adenosine Triphosphate Amino Acid Sequence Binding Sites Catalytic Domain Models, Molecular Molecular Sequence Data Phosphotransferases Protein Conformation Protein Folding metabolism chemistry metabolism|