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Related Concept Videos

Ligand Binding Sites02:40

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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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.
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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Ligand Binding and Linkage00:49

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Updated: Jun 5, 2025

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays
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Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

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Structure and Methyl-lysine Binding Selectivity of the HUSH Complex Subunit MPP8.

Nikos Nikolopoulos1, Shun-Ichiro Oda1, Daniil M Prigozhin2

  • 1Molecular Immunity Unit, Department of Medicine, University of Cambridge, MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK; Cambridge Institute of Therapeutic Immunology & Infectious Disease (CITIID), Department of Medicine, University of Cambridge, Cambridge CB2 0AW, UK.

Journal of Molecular Biology
|December 5, 2024
PubMed
Summary
This summary is machine-generated.

The Human Silencing Hub (HUSH) complex, crucial for genome stability, uses MPP8 structural insights to block harmful retroelements. This study reveals how HUSH components assemble and function to silence transposons.

Keywords:
H3K9 methyltransferaseLINE-1 retrotransposonepigenetic silencinghistone H3 lysine 9 methylation (H3K9me3)transcriptional repression

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Last Updated: Jun 5, 2025

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Genomics

Background:

  • The Human Silencing Hub (HUSH) complex protects the genome from retroelement expression.
  • HUSH functions by recognizing specific nascent transcripts and recruiting epigenetic modifiers.

Purpose of the Study:

  • To determine the structural basis of MPP8's role in HUSH complex assembly and function.
  • To elucidate the molecular mechanisms underlying HUSH-mediated transcriptional repression.

Main Methods:

  • Crystal structure determination of the MPP8 C-terminal domain (CTD).
  • AlphaFold3 modeling of the MPP8-TASOR complex.
  • Cell-based reporter assays to assess HUSH activity after mutagenesis.

Main Results:

  • The MPP8 CTD structure reveals ankyrin repeats and a PINIT-like domain.
  • AlphaFold3 accurately predicted interaction interfaces between MPP8 and TASOR, validated by mutation studies.
  • MPP8's chromodomain binds H3K9 methyltransferases, facilitating heterochromatin formation.

Conclusions:

  • Novel structural elements in MPP8 are essential for HUSH complex assembly and silencing.
  • MPP8 recruits H3K9 methyltransferases to promote heterochromatinization and control retrotransposons.
  • This work provides a structural framework for understanding HUSH-mediated genome defense.