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Literature summary for 1.14.14.14 extracted from

  • Di Nardo, G.; Di Venere, A.; Zhang, C.; Nicolai, E.; Castrignano, S.; Di Paola, L.; Gilardi, G.; Mei, G.
    Polymorphism on human aromatase affects protein dynamics and substrate binding spectroscopic evidence (2021), Biol. Direct, 16, 008 .
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
R264C single nuclotide polymorphism, impairs the correct binding of both substrate and inhibitor molecules. contrary to wild-type, mutant undergoes a less efficient packing process, suggesting a minor flexibility of the mobile segments Homo sapiens
R264H single nuclotide polymorphism, impairs the correct binding of both substrate and inhibitor molecules. contrary to wild-type, mutant undergoes a less efficient packing process, suggesting a minor flexibility of the mobile segments Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P11511
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General Information

General Information Comment Organism
metabolism CYP19A1 protein structure is organized in two main clusters, whose connectivity is altered by ligand binding. Upon substrate or inhibitor binding, the wild-type enzyme undergoes a conformational change leading to a more compact tertiary structure. In single-nucleotide polymorphisms R264C and R264H the exchange rates in the ligand-free and -bound forms are similar, and the quenching effect on tryptophan-224 observed upon ligand binding in the wild-type, is absent in both variants. Helices F and G between the two clusters that form the substrate channel to the active site have a connecting role Homo sapiens