5VYC

Crystal structure of the human 40S ribosomal subunit in complex with DENR-MCT-1.

This is a non-PDB format compatible entry.

Summary for 5VYC

• Entry DOI: 10.2210/pdb5vyc/pdb
• Descriptor: 40S ribosomal protein S19, 40S ribosomal protein S2, 40S ribosomal protein S6, ... (38 entities in total)
• Functional Keywords: ribosome, 40s subunit, denr-mct-1, pua
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 222
• Total formula weight: 7655375.20

Authors

Lomakin, I.B.,Stolboushkina, E.A.,Vaidya, A.T.,Garber, M.B.,Dmitriev, S.E.,Steitz, T.A. (deposition date: 2017-05-24, release date: 2017-07-19, Last modification date: 2024-12-25)

Primary citation

Lomakin, I.B.,Stolboushkina, E.A.,Vaidya, A.T.,Zhao, C.,Garber, M.B.,Dmitriev, S.E.,Steitz, T.A.
Crystal Structure of the Human Ribosome in Complex with DENR-MCT-1.
Cell Rep, 20:521-528, 2017

PubMed Abstract: The repertoire of the density-regulated protein (DENR) and the malignant T cell-amplified sequence 1 (MCT-1/MCTS1) oncoprotein was recently expanded to include translational control of a specific set of cancer-related mRNAs. DENR and MCT-1 form the heterodimer, which binds to the ribosome and operates at both translation initiation and reinitiation steps, though by a mechanism that is yet unclear. Here, we determined the crystal structure of the human small ribosomal subunit in complex with DENR-MCT-1. The structure reveals the location of the DENR-MCT-1 dimer bound to the small ribosomal subunit. The binding site of the C-terminal domain of DENR on the ribosome has a striking similarity with those of canonical initiation factor 1 (eIF1), which controls the fidelity of translation initiation and scanning. Our findings elucidate how the DENR-MCT-1 dimer interacts with the ribosome and have functional implications for the mechanism of unconventional translation initiation and reinitiation.

PubMed: 28723557
DOI: 10.1016/j.celrep.2017.06.025

Experimental method

X-RAY DIFFRACTION (6 Å)