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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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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Ligand Binding Sites02:40

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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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Related Experiment Video

Updated: Oct 22, 2025

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
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Rational Design of Constrained Peptides as Protein Interface Inhibitors.

Ramachandran Murali1, Hongtao Zhang2, Zheng Cai2

  • 1Cedars-Sinai Medical Center, Department of Biomedical Science, Research Division of Immunology, Los Angeles, CA 90211, USA.

Antibodies (Basel, Switzerland)
|August 27, 2021
PubMed
Summary
This summary is machine-generated.

Developing targeted therapeutics for protein-protein interactions is challenging. Our lab uses structural and computational biology to create peptide inhibitors and immunoadhesins for erbB and TNF receptors.

Keywords:
ErbBTNFcancerimmunoadhesionmimeticprotein-engineeringreceptor

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Area of Science:

  • Biochemistry and Structural Biology
  • Computational Biology and Drug Discovery
  • Molecular and Cellular Biology

Background:

  • Targeted therapeutics for protein-protein complexes face challenges due to undefined binding pockets and extensive interfaces.
  • Progress in developing small molecule drugs for these targets has been limited.
  • Protein-protein interactions are crucial in many cellular processes and disease pathways.

Purpose of the Study:

  • To present approaches for dissecting protein-protein complexes for therapeutic development.
  • To highlight the development and application of peptide inhibitors and immunoadhesins.
  • To focus on the erbB and tumor necrosis factor (TNF) receptor superfamilies.

Main Methods:

  • Utilizing a combination of structural biology techniques.
  • Employing computational biology approaches for analysis and design.
  • Dissecting protein-protein interactions within specific receptor superfamilies.

Main Results:

  • Demonstrated feasibility of developing peptide inhibitors for protein-protein interactions.
  • Showcased the application of immunoadhesins targeting cell surface receptors.
  • Successfully applied combined structural and computational biology methods.

Conclusions:

  • Structural and computational biology approaches can overcome challenges in targeting protein-protein complexes.
  • Peptide inhibitors and immunoadhesins represent viable therapeutic strategies.
  • Targeting erbB and TNF receptor superfamilies is achievable with these methods.