Ontology highlight
ABSTRACT:
SUBMITTER: Mertens C
PROVIDER: S-EPMC4672786 | biostudies-literature | 2015 Dec
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20151109 48
Crystallography of the cores of phosphotyrosine-activated dimers of STAT1 (132-713) and STAT3 (127-722) bound to a similar double-stranded deoxyoligonucleotide established the domain structure of the STATs and the structural basis for activation through tyrosine phosphorylation and dimerization. We reported earlier that mutants in the linker domain of STAT1 that connect the DNA-binding domain and SH2 domain can prevent transcriptional activation. Because of the pervasive importance of persistent ...[more]