ArticleScientific reports2019
Effects of point mutations in the binding pocket of the mouse major urinary protein MUP20 on ligand affinity and specificity.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Structural Remodeling of Phage φPNJ-6 Hoc Promotes Adhesion to the Intestinal Epithelium.Transboundary and emerging diseases · 2026Article
- Dissecting the effects of single amino acid substitutions in SARS-CoV-2 Mpro.Protein science : a publication of the Protein Society · 2025Article
- Proteomic analysis of horse hair extracts provides no evidence for the existence of a hypoallergenic Curly Horse breed.Clinical and translational allergy · 2024Article
- Characterizing and explaining the impact of disease-associated mutations in proteins without known structures or structural homologs.Briefings in bioinformatics · 2022Article
- New ligand-binding sites identified in the crystal structures of β-lactoglobulin complexes with desipramine.IUCrJ · 2022Article
- Regulation of Sexually Dimorphic Expression of Major Urinary Proteins.Frontiers in physiology · 2022Review
- Novel dynamic residue network analysis approaches to study allosteric modulation: SARS-CoV-2 MComputational and structural biotechnology journal · 2021Article
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Authors and funding
11 authors.
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Abstract
The mouse Major Urinary Proteins (MUPs) contain a conserved β-barrel structure with a characteristic central hydrophobic pocket that binds a variety of volatile compounds. After release of urine, these molecules are slowly emitted in the environment where they play an important role in chemical communication. MUPs are highly polymorphic and conformationally stable. They may be of interest in the construction of biosensor arrays capable of detection of a broad range of analytes. In this work, 14 critical amino acids in the binding pocket involved in ligand interactions were identified in MUP20 using in silico techniques and 7 MUP20 mutants were synthesised and characterised to produce a set of proteins with diverse ligand binding profiles to structurally different ligands. A single amino acid substitution in the binding pocket can dramatically change the MUPs binding affinity and ligand specificity. These results have great potential for the design of new biosensor and gas-sensor recognition elements.
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