6m3g

Crystal structure of human HPF1

Structural highlights

6m3g is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.57Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HPF1_HUMAN Acts as a cofactor for serine ADP-ribosylation by conferring serine specificity on PARP1 and PARP2: interacts with PARP1 and PARP2 and is able to change amino acid specificity toward serine (PubMed:28190768, PubMed:29480802). Promotes histone serine ADP-ribosylation in response to DNA damage, limiting DNA damage-induced PARP1 hyper-automodification, and ensuring genome stability (PubMed:27067600, PubMed:28190768). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:29480802). HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1 (PubMed:30257210).^[1] ^[2] ^[3] ^[4]

References

↑ Gibbs-Seymour I, Fontana P, Rack JGM, Ahel I. HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity. Mol Cell. 2016 May 5;62(3):432-442. doi: 10.1016/j.molcel.2016.03.008. Epub 2016 , Apr 7. PMID:27067600 doi:https://dx.doi.org/10.1016/j.molcel.2016.03.008
↑ Bonfiglio JJ, Fontana P, Zhang Q, Colby T, Gibbs-Seymour I, Atanassov I, Bartlett E, Zaja R, Ahel I, Matic I. Serine ADP-Ribosylation Depends on HPF1. Mol Cell. 2017 Mar 2;65(5):932-940.e6. doi: 10.1016/j.molcel.2017.01.003. Epub, 2017 Feb 9. PMID:28190768 doi:https://dx.doi.org/10.1016/j.molcel.2017.01.003
↑ Palazzo L, Leidecker O, Prokhorova E, Dauben H, Matic I, Ahel I. Serine is the major residue for ADP-ribosylation upon DNA damage. Elife. 2018 Feb 26;7. pii: 34334. doi: 10.7554/eLife.34334. PMID:29480802 doi:https://dx.doi.org/10.7554/eLife.34334
↑ Bartlett E, Bonfiglio JJ, Prokhorova E, Colby T, Zobel F, Ahel I, Matic I. Interplay of Histone Marks with Serine ADP-Ribosylation. Cell Rep. 2018 Sep 25;24(13):3488-3502.e5. doi: 10.1016/j.celrep.2018.08.092. PMID:30257210 doi:https://dx.doi.org/10.1016/j.celrep.2018.08.092

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OCA

[1] Gibbs-Seymour I, Fontana P, Rack JGM, Ahel I. HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity. Mol Cell. 2016 May 5;62(3):432-442. doi: 10.1016/j.molcel.2016.03.008. Epub 2016 , Apr 7. PMID:27067600 doi:https://dx.doi.org/10.1016/j.molcel.2016.03.008

[2] Bonfiglio JJ, Fontana P, Zhang Q, Colby T, Gibbs-Seymour I, Atanassov I, Bartlett E, Zaja R, Ahel I, Matic I. Serine ADP-Ribosylation Depends on HPF1. Mol Cell. 2017 Mar 2;65(5):932-940.e6. doi: 10.1016/j.molcel.2017.01.003. Epub, 2017 Feb 9. PMID:28190768 doi:https://dx.doi.org/10.1016/j.molcel.2017.01.003

[3] Palazzo L, Leidecker O, Prokhorova E, Dauben H, Matic I, Ahel I. Serine is the major residue for ADP-ribosylation upon DNA damage. Elife. 2018 Feb 26;7. pii: 34334. doi: 10.7554/eLife.34334. PMID:29480802 doi:https://dx.doi.org/10.7554/eLife.34334

[4] Bartlett E, Bonfiglio JJ, Prokhorova E, Colby T, Zobel F, Ahel I, Matic I. Interplay of Histone Marks with Serine ADP-Ribosylation. Cell Rep. 2018 Sep 25;24(13):3488-3502.e5. doi: 10.1016/j.celrep.2018.08.092. PMID:30257210 doi:https://dx.doi.org/10.1016/j.celrep.2018.08.092

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6m3g

Crystal structure of human HPF1

Structural highlights

Function

References

Contents

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