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Related Concept Videos

Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart, a...
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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DNA Helicases00:55

DNA Helicases

DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
Conserved Binding Sites01:49

Conserved Binding Sites

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Homologous Recombination02:31

Homologous Recombination

The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...

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Related Experiment Video

Updated: Jul 9, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Privileged scaffolds targeting reverse-turn and helix recognition.

Ye Che1, Garland R Marshall

  • 1Washington University, Center for Computational Biology and Department of Biochemistry and Molecular Biophysics, St. Louis, MO 63110, USA.

Expert Opinion on Therapeutic Targets
|December 14, 2007
PubMed
Summary

Researchers are developing small molecules to block protein-protein interactions, which are key in biology. This strategy uses "privileged structures" to mimic protein surfaces, aiding drug discovery for complex diseases.

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Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

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Related Experiment Videos

Last Updated: Jul 9, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Folding and Characterization of a Bio-responsive Robot from DNA Origami
07:59

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Published on: December 3, 2015

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Area of Science:

  • Medicinal Chemistry
  • Structural Biology
  • Drug Discovery

Background:

  • Protein-protein interactions (PPIs) are central to biological processes.
  • Large interaction surfaces of PPIs pose challenges for traditional drug discovery.
  • Many proteins involved in PPIs are intrinsically disordered until binding.

Purpose of the Study:

  • To identify small molecule leads for modulating PPIs.
  • To leverage common protein recognition motifs (e.g., helices, strands) for drug design.
  • To explore the 'privileged structure hypothesis' for designing PPI inhibitors.

Main Methods:

  • Reviewing strategies based on the 'privileged structure hypothesis'.
  • Highlighting advances in designing scaffolds targeting specific protein motifs.
  • Focusing on reverse-turn and helical recognition motifs.

Main Results:

  • Identification of 'drug-like' small molecule leads.
  • Demonstration of privileged scaffolds mimicking PPI surfaces.
  • Advances in targeting reverse-turn and helical recognition.

Conclusions:

  • Privileged scaffolds aid in understanding receptor-bound conformations.
  • These scaffolds provide non-peptidic, bioavailable starting points for drug optimization.
  • The strategy is effective for modulating protein-protein interactions.