Dataset Information


Interferon-inducible protein 16: insight into the interaction with tumor suppressor p53.

ABSTRACT: IFI16 is a member of the interferon-inducible HIN-200 family of nuclear proteins. It has been implicated in transcriptional regulation by modulating protein-protein interactions with p53 tumor suppressor protein and other transcription factors. However, the mechanisms of interaction remain unknown. Here, we report the crystal structures of both HIN-A and HIN-B domains of IFI16 determined at 2.0 and 2.35 Å resolution, respectively. Each HIN domain comprises a pair of tightly packed OB-fold subdomains that appear to act as a single unit. We show that both HIN domains of IFI16 are capable of enhancing p53-DNA complex formation and transcriptional activation via distinctive means. HIN-A domain binds to the basic C terminus of p53, whereas the HIN-B domain binds to the core DNA-binding region of p53. Both interactions are compatible with the DNA-bound state of p53 and together contribute to the effect of full-length IFI16 on p53-DNA complex formation and transcriptional activation.

PROVIDER: S-EPMC3760383 | BioStudies |

REPOSITORIES: biostudies

Similar Datasets

| S-EPMC4900677 | BioStudies
| S-EPMC3943098 | BioStudies
| S-EPMC6335826 | BioStudies
| S-EPMC3760141 | BioStudies
| S-EPMC3334467 | BioStudies
| S-EPMC7433898 | BioStudies
| S-EPMC6681451 | BioStudies
| S-EPMC6172465 | BioStudies
| S-EPMC3249514 | BioStudies
| S-EPMC2765525 | BioStudies