Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domain

Genes and Development

Volumn 20, Issue 24, 2006, Pages 3372-3381

  Mertens, Claudia ^a   Zhong, Minghao ^a   Krishnaraj, Ravi ^a   Zou, Wenxin ^b   Chen, Xiaomin ^b   Darnell Jr , James E ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

^b UNIVERSITY OF TEXAS   (United States)

Author keywords

Dephosphorylation; Reorientation; STAT1 domain

Indexed keywords

DIMER; DNA; EPITOPE; MONOMER; PHOSPHATASE; PHOSPHOTYROSINE; STAT1 PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; CRYSTALLOGRAPHY; DIMERIZATION; EXPRESSED SEQUENCE TAG; HUMAN; HUMAN CELL; MUTAGENESIS; NUCLEOTIDE SEQUENCE; PHENOTYPE; PREDICTION; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SPATIAL ORIENTATION;

EID: 33845718240     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.1485406     Document Type: Article

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