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Related Concept Videos

RNA Structure01:19

RNA Structure

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The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
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There are three main types of ribonucleic acid (RNA) involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three...
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RNA Structure01:23

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Overview
The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
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Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

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Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
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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.
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RNA Interference01:23

RNA Interference

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RNA interference (RNAi) is a process in which a small non-coding RNA molecule blocks the post-transcriptional expression of a gene by binding to its messenger RNA (mRNA) and preventing the protein from being translated.
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Nucleic Acids02:43

Nucleic Acids

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Nucleic acids are the most important macromolecules for the continuity of life. They carry the cell's genetic blueprint and carry instructions for its functioning.
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An Assay for Quantifying Protein-RNA Binding in Bacteria
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Structural insights into IMP2 dimerization and RNA binding.

Stephen A Zorc1, Paola Munoz-Tello2, Timothy O'Leary3

  • 1Department of Molecular Medicine, The Herbert Wertheim UF Scripps Institute for Biomedical Innovation & Technology, Jupiter, FL, USA; The Skaggs Graduate School of Chemical and Biological Science, The Scripps Research Institute, La Jolla, CA, USA.

Journal of Structural Biology
|September 14, 2025
PubMed
Summary
This summary is machine-generated.

Insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2) primarily forms dimers, with RNA binding altering its structure. Understanding full-length IGF2BP2 structure is key for drug discovery targeting cancer and metabolic diseases.

Keywords:
HDX-MSIGF2BP2IMP2RNA binding protein (RBP)SAXS

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Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2), also known as IMP2, is implicated in tumorigenesis and metabolic disorders.
  • Previous structural studies focused on individual domains of IMP2, leaving the full-length protein's structure and behavior uncharacterized.
  • Understanding the structure of full-length IMP2 is crucial for developing targeted drug discovery strategies.

Purpose of the Study:

  • To investigate the structural properties and oligomeric behavior of full-length IGF2BP2 (IMP2).
  • To determine the influence of RNA binding on the structure and oligomerization of IMP2.
  • To provide structural insights for potential therapeutic interventions targeting IMP2.

Main Methods:

  • Utilized biophysical techniques including mass photometry, hydrogen-deuterium exchange coupled with mass spectrometry (HDX-MS).
  • Employed small-angle X-ray scattering (SAXS) to model the structure of full-length IMP2.
  • Investigated the effects of RNA binding and varying ionic strength on IMP2 structure and oligomerization.

Main Results:

  • Full-length IMP2 exists in multiple oligomeric states, predominantly forming dimers.
  • SAXS data modeling suggests a head-to-tail dimeric orientation involving the KH34 and RRM1 domains.
  • RNA binding induces a pseudo-symmetric dimeric conformation distinct from the RNA-free state, and oligomerization is sensitive to ionic strength.

Conclusions:

  • This study presents the first structural characterization of full-length IMP2.
  • The findings reveal that IMP2 oligomerization is dynamic and modulated by RNA binding and ionic conditions.
  • These insights offer potential avenues for disrupting IMP2 function in disease contexts.