Latent membrane protein 1 (LMP1) is a 386-residue protein from Epstein-Barr virus. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: P03230.
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The mean pLDDT of this model is 48.4 (very low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 0% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 37% |
| Below 50 | Very low: often disordered regions | 56% |
What pLDDT means and how to read it
Acts as a CD40 functional homolog to prevent apoptosis of infected B-lymphocytes and drive their proliferation. Functions as a constitutively active tumor necrosis factor receptor that induces the activation of several signaling pathways, including those of the NF-kappa-B family (PubMed:25996949). LMP1 signaling leads to up-regulation of antiapoptotic proteins and provide growth signals in latently infected cells. Interacts with host UBE2I and subsequently affects the sumoylation state of several cellular proteins. For example, induces the sumoylation of host IRF7 thereby limiting its transcriptional activity and modulating the activation of innate immune responses. Also inhibits host…
Interacts (via PXQXT motif) with host tumor necrosis factor receptor-associated factor (TRAF) proteins TRAF1, TRAF2, TRAF3 and TRAF5 (PubMed:25996949). Interacts with human protein ZMYND11; leading to negatively regulate NF-kappa-B activation. Interacts with host UBE2I; this interaction induces the sumoylation of various cellular proteins (PubMed:21795333). Interacts with host IRF7. Interacts…
Host cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1CZY | X-ray | 2.0 Å | D/E=204-210 |
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