Ontology highlight
ABSTRACT:
SUBMITTER: Pang X
PROVIDER: S-EPMC4230710 | biostudies-literature | 2014 May
REPOSITORIES: biostudies-literature
Pang Xiaodong X Zhou Huan-Xiang HX
Journal of theoretical & computational chemistry 20140501 3
Protein phosphorylation is very common post-translational modification, catalyzed by kinases, for signaling and regulation. Phosphotyrosines frequently target SH2 domains. The spleen tyrosine kinase (Syk) is critical for tyrosine phosphorylation of multiple proteins and for regulation of important pathways. Phosphorylation of both Y342 and Y346 in Syk linker B is required for optimal signaling. The SH2 domains of Vav1 and PLC-γ both bind this doubly phosphorylated motif. Here we used a recently ...[more]