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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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.
Interaction domains in cell signaling
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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Related Experiment Video

Updated: Sep 3, 2025

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

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Shelterin is a dimeric complex with extensive structural heterogeneity.

John C Zinder1, Paul Dominic B Olinares2, Vladimir Svetlov3

  • 1Laboratory of Cell Biology and Genetics, The Rockefeller University, New York, NY 10065.

Proceedings of the National Academy of Sciences of the United States of America
|July 26, 2022
PubMed
Summary

Human shelterin, a key complex for telomere maintenance, exhibits significant conformational flexibility. This architectural variability is crucial for its diverse functions in protecting telomeres and regulating DNA.

Keywords:
AlphaFoldconformational heterogeneityelectron microscopyshelterintelomeres

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

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Related Experiment Videos

Last Updated: Sep 3, 2025

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Human shelterin is a multi-subunit protein complex essential for telomere maintenance.
  • It protects telomeres from DNA damage and regulates telomeric DNA.
  • Previous studies resolved individual shelterin domains but not the full complex architecture.

Purpose of the Study:

  • To determine the architecture and stoichiometry of the full human shelterin complex.
  • To investigate the conformational heterogeneity of shelterin and its subcomplexes.
  • To understand the functional implications of shelterin's structural variability.

Main Methods:

  • Purification of shelterin subcomplexes and reconstitution of the full complex.
  • Negative-stain electron microscopy (EM) and cross-linking mass spectrometry (XLMS).
  • AlphaFold modeling, mass photometry, and native mass spectrometry (MS).

Main Results:

  • Shelterin subcomplexes and the full complex display extensive conformational heterogeneity.
  • Variable positioning of key domains (POT1 DNA-binding, TPP1 OB-fold, TIN2 TRFH) was observed.
  • Dimeric stoichiometries were confirmed for shelterin and TRF1-containing subcomplexes, independent of DNA.

Conclusions:

  • Human shelterin exists in a multitude of conformations.
  • This architectural variability is likely essential for shelterin's diverse roles at telomeres.
  • Understanding shelterin's dynamic structure provides insights into telomere biology and disease.