7TGQ
Zinc finger antiviral protein (ZAP) central domain bound to ADP-ribose
Summary for 7TGQ
| Entry DOI | 10.2210/pdb7tgq/pdb |
| Related | 7KZH |
| Descriptor | Zinc finger CCCH-type antiviral protein 1, ZINC ION, ADENOSINE-5-DIPHOSPHORIBOSE, ... (5 entities in total) |
| Functional Keywords | restriction factor, antiviral protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 24129.22 |
| Authors | Pornillos, O.P. (deposition date: 2022-01-09, release date: 2022-02-02, Last modification date: 2023-10-25) |
| Primary citation | Xue, G.,Braczyk, K.,Goncalves-Carneiro, D.,Dawidziak, D.M.,Sanchez, K.,Ong, H.,Wan, Y.,Zadrozny, K.K.,Ganser-Pornillos, B.K.,Bieniasz, P.D.,Pornillos, O. Poly(ADP-ribose) potentiates ZAP antiviral activity. Plos Pathog., 18:e1009202-e1009202, 2022 Cited by PubMed Abstract: Zinc-finger antiviral protein (ZAP), also known as poly(ADP-ribose) polymerase 13 (PARP13), is an antiviral factor that selectively targets viral RNA for degradation. ZAP is active against both DNA and RNA viruses, including important human pathogens such as hepatitis B virus and type 1 human immunodeficiency virus (HIV-1). ZAP selectively binds CpG dinucleotides through its N-terminal RNA-binding domain, which consists of four zinc fingers. ZAP also contains a central region that consists of a fifth zinc finger and two WWE domains. Through structural and biochemical studies, we found that the fifth zinc finger and tandem WWEs of ZAP combine into a single integrated domain that binds to poly(ADP-ribose) (PAR), a cellular polynucleotide. PAR binding is mediated by the second WWE module of ZAP and likely involves specific recognition of an adenosine diphosphate-containing unit of PAR. Mutation of the PAR binding site in ZAP abrogates the interaction in vitro and diminishes ZAP activity against a CpG-rich HIV-1 reporter virus and murine leukemia virus. In cells, PAR facilitates formation of non-membranous sub-cellular compartments such as DNA repair foci, spindle poles and cytosolic RNA stress granules. Our results suggest that ZAP-mediated viral mRNA degradation is facilitated by PAR, and provides a biophysical rationale for the reported association of ZAP with RNA stress granules. PubMed: 35130321DOI: 10.1371/journal.ppat.1009202 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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