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Details on Person LANA1 forms oligomers that, based on in vitro studies, are l...
| Class:Id | Summation:9980859 |
|---|---|
| _displayName | LANA1 forms oligomers that, based on in vitro studies, are l... |
| _timestamp | 2026-06-04 17:21:24 |
| created | [InstanceEdit:9980857] Orlic-Milacic, Marija, 2026-02-03 |
| literatureReference | [LiteratureReference:9980856] Molecular basis for oligomeric-DNA binding and episome maintenance by KSHV LANA [LiteratureReference:9978530] A structural basis for BRD2/4-mediated host chromatin interaction and oligomer assembly of Kaposi sarcoma-associated herpesvirus and murine gammaherpesvirus LANA proteins [LiteratureReference:9980860] The 3D structure of Kaposi sarcoma herpesvirus LANA C-terminal domain bound to DNA |
| modified | [InstanceEdit:9987662] Stephan, Ralf, 2026-04-23 [InstanceEdit:9991269] Stephan, Ralf, 2026-06-04 |
| text | LANA1 forms oligomers that, based on in vitro studies, are likely decameric rings composed of a pentamer of LANA1 dimers, which interact with DNA through the outer ring surface (Domsic et al. 2013; Hellert et al. 2013). A further in vitro study has shown that LANA1 may form higher-order oligomers in the form of right-handed continuous spirals with ~5 LANA dimers per turn, which may contribute to the so-called LANA speckles, subnuclear HHV8 microdomains that are a hallmark of HHV8 latency (Hellert et al. 2015). The inner surface of LANA1 rings is positively charged, like the outer surface, and it was proposed that the inner surface is involved in non-specific interactions with the DNA, while the outer surface is involved in sequence-specific interactions (Hellert et al. 2015). The inner diameter of the LANA1 ring and the LANA1 spiral is sufficiently large to accommodate double-stranded DNA (Hellert et al. 2015). |
| (summation) | [Reaction:9980758] LANA1 oligomerizes on episome [Homo sapiens] |
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