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Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem

Authors Long, Jiafu HKUST affiliated (currently or previously)
Feng, Wei HKUST affiliated (currently or previously)
Wang, Rui
Chan, Ling Nga HKUST affiliated (currently or previously)
Ip, Fanny C.F. HKUST affiliated (currently or previously)
Xia, Jun View this author's profile
Ip, Nancy Y.Y. View this author's profile
Zhang, Mingjie View this author's profile
Issue Date 2005
Source Nature structural & molecular biology , v. 12, (8), 2005, AUG, p. 722-728
Summary Members of the X11/Mint family of multidomain adaptor proteins are composed of a divergent N terminus, a conserved PTB domain and a pair of C-terminal PDZ domains. Many proteins can interact with the PDZ tandem of X11 proteins, although the mechanism of such interactions is unclear. Here we show that the highly conserved C-terminal tail of X11 alpha folds back and inserts into the target-binding groove of the first PDZ domain. The binding of this tail occludes the binding of other target peptides. This autoinhibited conformation of X11 requires that the two PDZ domains and the entire C-terminal tail be covalently connected to form an integral structural unit. The autoinhibited conformation of the X11 PDZ tandem provides a mechanistic explanation for the unique target-binding properties of the protein and hints at potential regulatory mechanisms for the X11-target interactions.
ISSN 1545-9985
Language English
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