ArticleBiophysical journal2006
Cooperative fluctuations point to the dimerization interface of p53 core domain.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Structural and Drug Targeting Insights on Mutant p53.Cancers · 2021Review
- Modulation of Toroidal Proteins Dynamics in Favor of Functional Mechanisms upon Ligand Binding.Biophysical journal · 2020Article
- Comparative Study of Elastic Network Model and Protein Contact Network for Protein Complexes: The Hemoglobin Case.BioMed research international · 2017Article
- Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family members.PLoS computational biology · 2011Article
- Influence of oligomerization on the dynamics of G-protein coupled receptors as assessed by normal mode analysis.Proteins · 2008Article
- Probing potential binding modes of the p53 tetramer to DNA based on the symmetries encoded in p53 response elements.Nucleic acids research · 2007Article
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Authors and funding
3 authors.
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Abstract
Elastic network models are used for investigation of the p53 core domain functional dynamics. Global modes of motion indicate high positive correlations for residue fluctuations across the A-B interface, which are not observed at the B-C interface. Major hinge formation is observed at the A-B interface upon dimerization indicating stability of the A-B dimer. These findings imply A-B as the native dimerization interface, whereas B-C is the crystal interface. The A-B dimer exhibits an opening-closing motion about DNA, supporting the previously suggested clamp-like model of nonspecific DNA binding followed by diffusion. Monomer A has limited positive correlations with DNA, while monomer B exhibits high positive correlations with DNA in the functionally significant slow modes. Thus, monomer B might seem to maintain the stability of the dimer-DNA complex by forming the relatively fixed arm of the dimer clamp, whereas the other arm of the clamp, monomer A, might allow sliding via continuous association/dissociation mechanisms.
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