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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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lncRNA - Long Non-coding RNAs02:39

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In humans, more than 80% of the genome gets transcribed. However, only around 2% of the genome codes for proteins. The remaining part produces non-coding RNAs which includes ribosomal RNAs, transfer RNAs, telomerase RNAs, and regulatory RNAs, among other types. A large number of regulatory non-coding RNAs have been classified into two groups depending upon their length – small non-coding RNAs, such as microRNA, which are less than 200 nucleotides in length, and long non-coding RNA...
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Assembly of Signaling Complexes01:30

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Conserved Binding Sites01:49

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Related Experiment Video

Updated: Nov 27, 2025

Identification of RNAs Engaged in Direct RNA-RNA Interaction with a Long Non-Coding RNA
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Identification of RNAs Engaged in Direct RNA-RNA Interaction with a Long Non-Coding RNA

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Deciphering LncRNA-protein interactions using docking complexes.

Renuka Suravajhala1, Sonal Gupta2,3, Narayan Kumar4

  • 1Department of Chemistry, School of Basic Science, Manipal University, Manipal, India.

Journal of Biomolecular Structure & Dynamics
|December 7, 2020
PubMed
Summary
This summary is machine-generated.

Understanding RNA-protein interactions is key for deciphering biological mechanisms. This study models binding sites between a specific long non-coding RNA (lncRNA) and a protein to investigate a rare disease.

Keywords:
binding sitesdocking complexeslncRNAsprotein targetsstructural modeling

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RNA Pull-down Procedure to Identify RNA Targets of a Long Non-coding RNA
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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • RNA-protein interactions are crucial for gene regulation, including transcription and translation.
  • Non-coding RNAs (ncRNAs) have limited functional understanding due to their lack of coding potential.
  • RNA-binding proteins associated with ncRNAs play vital roles in cellular processes like maturation and nuclear export.

Purpose of the Study:

  • To develop refined methods for understanding protein-RNA interactions.
  • To infer binding sites between long non-coding RNA (lncRNA) NONHSAT02007 and protein KIF13A.
  • To investigate these interactions in the context of a rare disease phenotype.

Main Methods:

  • Computational docking model utilized to predict binding sites.
  • Analysis focused on the interaction between lncRNA NONHSAT02007 and protein KIF13A.

Main Results:

  • A docking model was successfully applied to predict potential binding sites.
  • Identified potential interaction sites between lncRNA NONHSAT02007 and KIF13A.

Conclusions:

  • The developed docking model provides a refined approach to study protein-RNA interactions.
  • Understanding these specific interactions may offer insights into rare disease mechanisms.