Role of Arg243 and His239 Residues in the Recognition of Damaged Nucleotides by Human Uracil-DNA Glycosylase SMUG1

Human uracil-DNA glycosylase SMUG1 removes uracil residues and some other noncanonical or damaged bases from DNA. Despite the functional importance of this enzyme, its X-ray structure is still unavailable. Previously, we performed homology modeling of human SMUG1 structure and suggested the roles of...

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Veröffentlicht in:	Biochemistry (Moscow) 2020-05, Vol.85 (5), p.594-603
Hauptverfasser:	Iakovlev, D. A., Alekseeva, I. V., Kuznetsov, N. A., Fedorova, O. S.
Format:	Artikel
Sprache:	eng
Schlagworte:	2-Aminopurine Amino Acid Sequence Amino acids Analysis Arginine - chemistry Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Catalysis Catalytic Domain Chemical compounds Deoxyribonucleic acid DNA DNA Damage DNA glycosylase DNA Repair Energy transfer Enzymes Ethylenediaminetetraacetic acid Fluorescence Fluorescence resonance energy transfer Fluorophores Histidine - chemistry Homology Humans Intermediates Kinetics Life Sciences Microbiology Molecular Dynamics Simulation Nucleotides Parameter identification Pyrimidines Reaction intermediates Reaction kinetics Recognition Residues Sequence Homology SMUG1 protein Substrate Specificity Substrates Tryptophan Uracil Uracil - metabolism Uracil-DNA glycosidase Uracil-DNA Glycosidase - chemistry Uracil-DNA Glycosidase - genetics Uracil-DNA Glycosidase - metabolism
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