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Related Concept Videos

Ribosomes01:27

Ribosomes

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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome...
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Ribosomes01:27

Ribosomes

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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome...
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Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Termination of Translation01:44

Termination of Translation

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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Nucleic Acid Structure01:25

Nucleic Acid Structure

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The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA...
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Related Experiment Video

Updated: Feb 26, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
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Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

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Crystal Structure of the Human Ribosome in Complex with DENR-MCT-1.

Ivan B Lomakin1, Elena A Stolboushkina2, Anand T Vaidya1

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.

Cell Reports
|July 21, 2017
PubMed
Summary

The density-regulated protein (DENR)-malignant T cell-amplified sequence 1 (MCT-1) complex binds ribosomes to control cancer-related mRNA translation. Structural analysis reveals its ribosome interaction site, offering insights into translation initiation mechanisms.

Keywords:
density regulated proteinmalignant T cell-amplified sequence 1protein synthesisribosometranslation initiationtranslation reinitiation

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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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Rapid Isolation of the Mitoribosome from HEK Cells
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Rapid Isolation of the Mitoribosome from HEK Cells

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Related Experiment Videos

Last Updated: Feb 26, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
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Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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Rapid Isolation of the Mitoribosome from HEK Cells
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Rapid Isolation of the Mitoribosome from HEK Cells

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cancer Research

Background:

  • Density-regulated protein (DENR) and malignant T cell-amplified sequence 1 (MCT-1/MCTS1) oncoprotein regulate cancer-related mRNA translation.
  • DENR and MCT-1 form a heterodimer that binds ribosomes, influencing translation initiation and reinitiation.

Purpose of the Study:

  • To determine the crystal structure of the human small ribosomal subunit in complex with the DENR-MCT-1 dimer.
  • To elucidate the binding site and mechanism of DENR-MCT-1 interaction with the ribosome.

Main Methods:

  • X-ray crystallography
  • Structural analysis of protein-ribosome complex

Main Results:

  • The crystal structure of the human small ribosomal subunit complexed with DENR-MCT-1 was determined.
  • The DENR-MCT-1 dimer binds to the small ribosomal subunit.
  • The DENR C-terminal domain binding site on the ribosome resembles that of translation initiation factor 1 (eIF1).

Conclusions:

  • The study reveals the structural basis of DENR-MCT-1 interaction with the ribosome.
  • Findings provide insights into the mechanism of unconventional translation initiation and reinitiation.
  • This structural information has implications for understanding cancer-related translational control.