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The structure of SDS22 provides insights into the mechanism of heterodimer formation with PP1
Author(s) -
Choy Meng S.,
Bolik-Coulon Nicolas,
Archuleta Tara L.,
Peti Wolfgang,
Page Rebecca
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18016503
Subject(s) - protein phosphatase 1 , regulator , biology , phosphatase , microbiology and biotechnology , intrinsically disordered proteins , protein structure , computational biology , biophysics , chemistry , biochemistry , phosphorylation , gene
Protein phosphatase 1 (PP1) dephosphorylates hundreds of key biological targets by associating with nearly 200 regulatory proteins to form highly specific holoenzymes. The vast majority of regulators are intrinsically disordered proteins (IDPs) and bind PP1 via short linear motifs within their intrinsically disordered regions. One of the most ancient PP1 regulators is SDS22, a protein that is conserved from yeast to mammals. Sequence analysis of SDS22 revealed that it is a leucine‐rich repeat (LRR) protein, suggesting that SDS22, unlike nearly every other known PP1 regulator, is not an IDP but instead is fully structured. Here, the 2.9 Å resolution crystal structure of human SDS22 in space group P 2 1 2 1 2 1 is reported. SDS22 adopts an LRR fold with the horseshoe‐like curvature typical for this family of proteins. The structure results in surfaces with distinct chemical characteristics that are likely to be critical for PP1 binding.