{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T01:57:11Z","timestamp":1760147831403,"version":"build-2065373602"},"reference-count":12,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2023,3,3]],"date-time":"2023-03-03T00:00:00Z","timestamp":1677801600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"publisher","award":["22-24-00699"],"award-info":[{"award-number":["22-24-00699"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Data"],"abstract":"<jats:p>Fe(II)\/2OG-dependent dioxygenases of the AlkB family catalyze a direct removal of alkylated damages in the course of DNA and RNA repair. A human homolog of the E. coli AlkB ALKBH3 protein is able to hydroxylate N1-methyladenine, N3-methylcytosine, and N1-methylguanine in single-stranded DNA and RNA. Due to its contribution to an antitumor drug resistance, this enzyme is considered a promising therapeutic target. The elucidation of ALKBH3\u2019s structural peculiarities is important to establish a detailed mechanism of damaged DNA recognition and processing, as well as to the development of specific inhibitors. This work presents new data on the wild type ALKBH3 protein and its four mutant forms (Y143F, Y143A, L177A, and H191A) obtained by circular dichroism (CD) spectroscopy. The dataset includes the CD spectra of proteins measured at different temperatures and a 3D visualization of the ALKBH3\u2013DNA complex where the mutated amino acid residues are marked. These results show how substitution of the key amino acids influences a secondary structure content of the protein.<\/jats:p>","DOI":"10.3390\/data8030057","type":"journal-article","created":{"date-parts":[[2023,3,6]],"date-time":"2023-03-06T04:29:58Z","timestamp":1678076998000},"page":"57","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Dataset for Spectroscopic, Structural and Dynamic Analysis of Human Fe(II)\/2OG-Dependent Dioxygenase ALKBH3"],"prefix":"10.3390","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6832-2522","authenticated-orcid":false,"given":"Lyubov Yu.","family":"Kanazhevskaya","sequence":"first","affiliation":[{"name":"Institute of Chemical Biology and Fundamental Medicine (ICBFM), 8 Lavrentiev Ave., 630090 Novosibirsk, Russia"}]},{"given":"Alexey A.","family":"Gorbunov","sequence":"additional","affiliation":[{"name":"Department of Natural Sciences, Novosibirsk State University, 1 Pirogova St., 630090 Novosibirsk, Russia"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0695-6698","authenticated-orcid":false,"given":"Polina V.","family":"Zhdanova","sequence":"additional","affiliation":[{"name":"Institute of Chemical Biology and Fundamental Medicine (ICBFM), 8 Lavrentiev Ave., 630090 Novosibirsk, Russia"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2577-2184","authenticated-orcid":false,"given":"Vladimir V.","family":"Koval","sequence":"additional","affiliation":[{"name":"Institute of Chemical Biology and Fundamental Medicine (ICBFM), 8 Lavrentiev Ave., 630090 Novosibirsk, Russia"},{"name":"Department of Natural Sciences, Novosibirsk State University, 1 Pirogova St., 630090 Novosibirsk, Russia"}]}],"member":"1968","published-online":{"date-parts":[[2023,3,3]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"20734","DOI":"10.1074\/jbc.R115.656462","article-title":"The AlkB Family of Fe(II)\/alpha-Ketoglutarate-dependent Dioxygenases: Repairing Nucleic Acid Alkylation Damage and Beyond","volume":"290","author":"Fedeles","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1038\/nature01363","article-title":"Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA","volume":"421","author":"Aas","year":"2003","journal-title":"Nature"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1038\/sj.bjc.6606012","article-title":"ALKBH3, a human AlkB homologue, contributes to cell survival in human non-small-cell lung cancer","volume":"104","author":"Tasaki","year":"2011","journal-title":"Br. J. Cancer"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"5247","DOI":"10.1158\/1078-0432.CCR-12-0955","article-title":"ALKBH3 contributes to survival and angiogenesis of human urothelial carcinoma cells through NADPH oxidase and tweak\/Fn14\/VEGF signals","volume":"18","author":"Shimada","year":"2012","journal-title":"Clin. Cancer Res."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"4364","DOI":"10.1039\/c0cs00203h","article-title":"Inhibition of 2-oxoglutarate dependent oxygenases","volume":"40","author":"Rose","year":"2011","journal-title":"Chem. Soc. Rev."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1038\/sj.emboj.7601219","article-title":"Human ABH3 structure and key residues for oxidative demethylation to reverse DNA\/RNA damage","volume":"25","author":"Sundheim","year":"2006","journal-title":"EMBO J."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF chimera\u2014A visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1006\/abio.2000.4880","article-title":"Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set","volume":"287","author":"Sreerama","year":"2000","journal-title":"Anal. Biochem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"E3095","DOI":"10.1073\/pnas.1500851112","article-title":"Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy","volume":"112","author":"Micsonai","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"3334","DOI":"10.1021\/bi201699e","article-title":"Changes in protein dynamics of the DNA repair dioxygenase AlkB upon binding of Fe(2+) and 2-oxoglutarate","volume":"51","author":"Bleijlevens","year":"2012","journal-title":"Biochemistry"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.phytochem.2003.08.016","article-title":"Cupins: The most functionally diverse protein superfamily?","volume":"65","author":"Dunwell","year":"2004","journal-title":"Phytochemistry"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1002\/prot.340060202","article-title":"The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure","volume":"6","author":"Kuwajima","year":"1989","journal-title":"Proteins"}],"container-title":["Data"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2306-5729\/8\/3\/57\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T18:47:29Z","timestamp":1760122049000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2306-5729\/8\/3\/57"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,3,3]]},"references-count":12,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2023,3]]}},"alternative-id":["data8030057"],"URL":"https:\/\/doi.org\/10.3390\/data8030057","relation":{},"ISSN":["2306-5729"],"issn-type":[{"type":"electronic","value":"2306-5729"}],"subject":[],"published":{"date-parts":[[2023,3,3]]}}}