ArticleThe Journal of biological chemistry2011
Biophysical characterization of the complex between human papillomavirus E6 protein and synapse-associated protein 97.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Graph neural network integrated with pretrained protein language model for predicting human-virus protein-protein interactions.Briefings in bioinformatics · 2025Article
- Article
- Human Serine Racemase Weakly Binds the Third PDZ Domain of PSD-95.International journal of molecular sciences · 2022Article
- HPV E6 and E7 oncoproteins cooperatively alter the expression of Disc Large 1 polarity protein in epithelial cells.BMC cancer · 2020Article
- Review
- Improved affinity at the cost of decreased specificity: a recurring theme in PDZ-peptide interactions.Scientific reports · 2016Article
- Degradation of Human PDZ-Proteins by Human Alphapapillomaviruses Represents an Evolutionary Adaptation to a Novel Cellular Niche.PLoS pathogens · 2015Article
- Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus.Scientific reports · 2015Article
- Targeting protein-protein interactions with trimeric ligands: high affinity inhibitors of the MAGUK protein family.PloS one · 2015Article
- Allosteric conformational barcodes direct signaling in the cell.Structure (London, England : 1993) · 2013Review
- Change in allosteric network affects binding affinities of PDZ domains: analysis through perturbation response scanning.PLoS computational biology · 2011Review
- A switch I mutant of Cdc42 exhibits less conformational freedom.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The E6 protein of human papillomavirus (HPV) exhibits complex interaction patterns with several host proteins, and their roles in HPV-mediated oncogenesis have proved challenging to study. Here we use several biophysical techniques to explore the binding of E6 to the three PDZ domains of the tumor suppressor protein synapse-associated protein 97 (SAP97). All of the potential binding sites in SAP97 bind E6 with micromolar affinity. The dissociation rate constants govern the different affinities of HPV16 and HPV18 E6 for SAP97. Unexpectedly, binding is not mutually exclusive, and all three PDZ domains can simultaneously bind E6. Intriguingly, this quaternary complex has the same apparent hydrodynamic volume as the unliganded PDZ region, suggesting that a conformational change occurs in the PDZ region upon binding, a conclusion supported by kinetic experiments. Using NMR, we discovered a new mode of interaction between E6 and PDZ: a subset of residues distal to the canonical binding pocket in the PDZ(2) domain exhibited noncanonical interactions with the E6 protein. This is consistent with a larger proportion of the protein surface defining binding specificity, as compared with that reported previously.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.