Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)

Poly(ADP-ribosyl)ation represents an important post-translational modification in higher eukaryotes. Several DNA repair/checkpoint proteins possess specific PAR-Binding Zinc finger (PBZ) modules critical for function. Here, we present solution structures of the two PBZ modules of APLF (Aprataxin and...

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Autores principales: Eustermann, Sebastian, Brockmann, Christoph, Mehrotra, Pawan Vinod, Yang, Ji-Chun, Loakes, David, West, Stephen C., Ahel, Ivan, Neuhaus, David
Formato: Texto
Lenguaje:English
Publicado: 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2912505/
https://www.ncbi.nlm.nih.gov/pubmed/20098424
http://dx.doi.org/10.1038/nsmb.1747
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author Eustermann, Sebastian
Brockmann, Christoph
Mehrotra, Pawan Vinod
Yang, Ji-Chun
Loakes, David
West, Stephen C.
Ahel, Ivan
Neuhaus, David
author_facet Eustermann, Sebastian
Brockmann, Christoph
Mehrotra, Pawan Vinod
Yang, Ji-Chun
Loakes, David
West, Stephen C.
Ahel, Ivan
Neuhaus, David
author_sort Eustermann, Sebastian
collection PubMed
description Poly(ADP-ribosyl)ation represents an important post-translational modification in higher eukaryotes. Several DNA repair/checkpoint proteins possess specific PAR-Binding Zinc finger (PBZ) modules critical for function. Here, we present solution structures of the two PBZ modules of APLF (Aprataxin and PNK-like factor), revealing a novel type of zinc finger. By combining in vivo PAR-binding data with NMR interaction data using PAR fragments, we suggest a structural basis for PBZ-PAR recognition.
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spelling pubmed-29125052010-08-01 Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose) Eustermann, Sebastian Brockmann, Christoph Mehrotra, Pawan Vinod Yang, Ji-Chun Loakes, David West, Stephen C. Ahel, Ivan Neuhaus, David Nat Struct Mol Biol Article Poly(ADP-ribosyl)ation represents an important post-translational modification in higher eukaryotes. Several DNA repair/checkpoint proteins possess specific PAR-Binding Zinc finger (PBZ) modules critical for function. Here, we present solution structures of the two PBZ modules of APLF (Aprataxin and PNK-like factor), revealing a novel type of zinc finger. By combining in vivo PAR-binding data with NMR interaction data using PAR fragments, we suggest a structural basis for PBZ-PAR recognition. 2010-01-24 2010-02 /pmc/articles/PMC2912505/ /pubmed/20098424 http://dx.doi.org/10.1038/nsmb.1747 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Eustermann, Sebastian
Brockmann, Christoph
Mehrotra, Pawan Vinod
Yang, Ji-Chun
Loakes, David
West, Stephen C.
Ahel, Ivan
Neuhaus, David
Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)
title Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)
title_full Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)
title_fullStr Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)
title_full_unstemmed Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)
title_short Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)
title_sort solution structures of the two pbz domains from human aplf and their interaction with poly(adp-ribose)
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2912505/
https://www.ncbi.nlm.nih.gov/pubmed/20098424
http://dx.doi.org/10.1038/nsmb.1747
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