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

Author

Mertens, Claudia, Minghao Zhong, Krishnaraj, Ravi, Wenxin Zou, and Xiaomin Chen

Subjects
Phosphorylation -- Research, Tyrosine metabolism -- Research, DNA-ligand interactions -- Research, Biological sciences
Abstract

The experiments that infer a radical reorientation of tyrosine-phosphorylated parallel STAT1 dimers to an antiparallel form, allowing easy access to a phosphatase, are reported. The analysis has suggested that spatial mobility of the N-terminal domain (ND) on its tether is needed for parallel-to-antiparallel reorientation of the phosphorylated core to allow efficient dephosphorylation and the ND has a vital role in promoting the dephosphorylation.

Published
2006

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