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6zv2

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TFIIS N-terminal domain (TND) from human PPP1R10

Structural highlights

6zv2 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PP1RA_HUMAN Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers (By similarity).^[1]

Publication Abstract from PubMed

[Figure: see text].

A ubiquitous disordered protein interaction module orchestrates transcription elongation.,Cermakova K, Demeulemeester J, Lux V, Nedomova M, Goldman SR, Smith EA, Srb P, Hexnerova R, Fabry M, Madlikova M, Horejsi M, De Rijck J, Debyser Z, Adelman K, Hodges HC, Veverka V Science. 2021 Nov 26;374(6571):1113-1121. doi: 10.1126/science.abe2913. Epub 2021, Nov 25. PMID:34822292^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kreivi JP, Trinkle-Mulcahy L, Lyon CE, Morrice NA, Cohen P, Lamond AI. Purification and characterisation of p99, a nuclear modulator of protein phosphatase 1 activity. FEBS Lett. 1997 Dec 22;420(1):57-62. PMID:9450550
↑ Cermakova K, Demeulemeester J, Lux V, Nedomova M, Goldman SR, Smith EA, Srb P, Hexnerova R, Fabry M, Madlikova M, Horejsi M, De Rijck J, Debyser Z, Adelman K, Hodges HC, Veverka V. A ubiquitous disordered protein interaction module orchestrates transcription elongation. Science. 2021 Nov 26;374(6571):1113-1121. doi: 10.1126/science.abe2913. Epub 2021, Nov 25. PMID:34822292 doi:http://dx.doi.org/10.1126/science.abe2913