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PDBsum entry 3v4y
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Contents |
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293 a.a.
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41 a.a.
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39 a.a.
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39 a.a.
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43 a.a.
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References listed in PDB file
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Key reference
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Title
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The molecular basis for substrate specificity of the nuclear nipp1:pp1 holoenzyme.
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Authors
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N.O'Connell,
S.R.Nichols,
E.Heroes,
M.Beullens,
M.Bollen,
W.Peti,
R.Page.
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Ref.
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Structure, 2012,
20,
1746-1756.
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PubMed id
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Abstract
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Regulation of protein phosphatase 1 (PP1) is controlled by a diverse array of
regulatory proteins. However, how these proteins direct PP1 specificity is not
well understood. More than one-third of the nuclear pool of PP1 forms a
holoenzyme with the nuclear inhibitor of PP1, NIPP1, to regulate chromatin
remodeling, among other essential biological functions. Here, we show that the
PP1-binding domain of NIPP1 is an intrinsically disordered protein, which binds
PP1 in an unexpected manner. NIPP1 forms an α helix that engages PP1 at a
unique interaction site, using polar rather than hydrophobic contacts.
Importantly, the structure also reveals a shared PP1 interaction site outside of
the RVxF motif, the ΦΦ motif. Finally, we show that NIPP1:PP1 substrate
selectivity is determined by altered electrostatics and enhanced substrate
localization. Together, our results provide the molecular basis by which NIPP1
directs PP1 substrate specificity in the nucleus.
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