9LAF
Crystal structure of Elongin BC-EPOP peptide
Summary for 9LAF
| Entry DOI | 10.2210/pdb9laf/pdb |
| Descriptor | Elongin-B, Elongin-C, Elongin BC and Polycomb repressive complex 2-associated protein, ... (4 entities in total) |
| Functional Keywords | epop, elongin b, elongin c, transcription |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 25551.30 |
| Authors | |
| Primary citation | Kim, S.,Yeo, H.,Lee, B.I. Structural analysis of EPOP BC-box binding to the elongin BC complex. Biochem.Biophys.Res.Commun., 759:151691-151691, 2025 Cited by PubMed Abstract: The elongin BC complex (ELOBC) interacts with BC-box-containing proteins and plays a role in various cellular processes, including transcriptional regulation and ubiquitination. Elongin BC and polycomb repressive complex 2-associated protein (EPOP) contains a BC-box motif in its N-terminal region and influences cancer cell proliferation and differentiation. A previous study showed that a BC-box containing an EPOP-derived peptide suppresses cancer cell growth and induces apoptosis by disrupting the interaction between the ELOBC and its partner proteins. Here, we report the crystal structure of the EPOP BC-box peptide bound to the ELOBC and compare it with the structures of other BC-box-containing proteins in complex with the ELOBC. The overall structure of interactions between the BC-box and the ELOC was similar across different complexes, indicating a conserved binding mode. Our structural analysis revealed that the strictly conserved leucine residue (Leu40) within the BC-box of EPOP, which was previously suggested to be critical for interactions between the BC-box and the ELOC, was deeply embedded in the hydrophobic pocket of the ELOC protein. This study provided structural insights into BC-box-mediated protein-protein interactions and may serve as a fundamental resource for developing small molecules that modulate the interactions between ELOBC and BC-box-containing proteins. PubMed: 40153999DOI: 10.1016/j.bbrc.2025.151691 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.14 Å) |
Structure validation
Download full validation report






