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9LAF

Crystal structure of Elongin BC-EPOP peptide

Summary for 9LAF
Entry DOI10.2210/pdb9laf/pdb
DescriptorElongin-B, Elongin-C, Elongin BC and Polycomb repressive complex 2-associated protein, ... (4 entities in total)
Functional Keywordsepop, elongin b, elongin c, transcription
Biological sourceHomo sapiens (human)
More
Total number of polymer chains3
Total formula weight25551.30
Authors
Kim, S.,Lee, B.I. (deposition date: 2025-01-02, release date: 2025-05-21)
Primary citationKim, 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: 40153999
DOI: 10.1016/j.bbrc.2025.151691
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.14 Å)
Structure validation

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