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Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
These groups modify specific amino acids in a protein.
DNA Damage can Stall the Cell Cycle02:36

DNA Damage can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...
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...
DNA Damage Can Stall the Cell Cycle02:36

DNA Damage Can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...

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High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy
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Four p53 DNA-binding domain peptides bind natural p53-response elements and bend the DNA

P Balagurumoorthy1, H Sakamoto, M S Lewis

  • 1Department of Biochemistry, University of Nevada Reno 89557-0014, USA.

Proceedings of the National Academy of Sciences of the United States of America
|September 12, 1995
PubMed
Summary

The p53 DNA-binding domain (p53DBD) binds DNA cooperatively, forming a 4:1 complex that bends DNA significantly. This suggests p53DBD may contribute to p53 tetramerization.

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Last Updated: Jul 11, 2026

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Previous studies elucidated the p53 DNA-binding domain (p53DBD) and tetramerization domain structures.
  • However, the interplay between these domains and their synergistic functions remained unclear.

Purpose of the Study:

  • To investigate the DNA-binding properties of the p53DBD.
  • To understand its interaction with biologically relevant DNA response elements.

Main Methods:

  • DNA circularization assays.
  • Analytical ultracentrifugation.

Main Results:

  • The p53DBD binds strongly and cooperatively to DNA with a 4:1 stoichiometry.
  • Complex formation induces a significant axial bend (at least 60 degrees) in DNA response elements.
  • A high-affinity binding constant (Kd = 8.3 x 10^-8 M) was determined for the WAF1 element.

Conclusions:

  • The p53DBD can form a stable 4:1 nucleoprotein complex, mirroring wild-type p53 stoichiometry.
  • This binding induces substantial DNA conformational changes.
  • These findings suggest a potential role for the p53DBD in p53 tetramerization.