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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Structural Basis for Non-classical WIN Peptides Recognition by WDR5.

Yang Yang1, Yan Pan1, Qingying Wang1

  • 1School of Life Sciences and Medical Engineering, Anhui University, Hefei, Anhui 230601, China.

Journal of Molecular Biology
|February 1, 2026
PubMed
Summary
This summary is machine-generated.

Researchers discovered new ways WD repeat-containing protein 5 (WDR5) can bind to molecules, revealing unexpected flexibility. This finding offers new strategies for developing WDR5 inhibitors to target cancer.

Keywords:
WDR5WIN siteX-ray crystallographyprotein–protein interactionstrans-binding mode

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Oncology

Background:

  • WD repeat-containing protein 5 (WDR5) is a key scaffold in chromatin modification complexes.
  • The WDR5-interacting (WIN) site is crucial for WDR5's interactions with partner proteins.
  • WDR5 dysregulation is linked to cancer, making the WIN site a therapeutic target.

Purpose of the Study:

  • To explore novel binding geometries of the WDR5 WIN site beyond canonical interactions.
  • To investigate the structural basis for alternative WDR5 recognition modes.
  • To inform the design of next-generation WDR5 inhibitors.

Main Methods:

  • High-resolution crystal structure determination of WDR5 with arginine-containing peptide probes.
  • Isothermal titration calorimetry (ITC) to assess binding affinities.
  • Structural analysis of peptide binding to the WIN site and adjacent S7 pocket.

Main Results:

  • Two previously unrecognized binding modes of peptides to the WDR5 WIN site were identified.
  • One peptide bound in an extended conformation, bridging the WIN and S7 sites.
  • Another peptide adopted a reversed (trans-WIN) orientation, engaging both sites.
  • Moderate and specific binding affinities were confirmed by ITC.

Conclusions:

  • The WDR5 WIN site exhibits significant conformational adaptability.
  • WDR5 recognition extends beyond the canonical motif, accommodating diverse binding topologies.
  • These findings provide a framework for designing WDR5 inhibitors targeting alternative binding modes and multi-site engagement for cancer therapy.