1H, 15N, 13C resonance assignments for proteasome shuttle factor hHR23a
Author:
Funder
Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research to K.J.W.
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
https://link.springer.com/content/pdf/10.1007/s12104-023-10157-z.pdf
Reference27 articles.
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2. Bertolaet BL, Clarke DJ, Wolff M, Watson MH, Henze M, Divita G et al (2001) UBA domains of DNA damage-inducible proteins interact with ubiquitin. Nat Struct Biol 8(5):417–422. https://doi.org/10.1038/87575
3. Byeon IL, Jung J, Byeon CH, DeLucia M, Ahn J, Gronenborn AM (2020) Complete (1)H, (13)C, (15)N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223–363). Biomol NMR Assign 14(1):13–17. https://doi.org/10.1007/s12104-019-09913-x
4. Byeon IL, Calero G, Wu Y, Byeon CH, Jung J, DeLucia M et al (2021) Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A. Nat Commun 12(1):6864. https://doi.org/10.1038/s41467-021-27009-w
5. Chen X, Walters KJ (2012) Identifying and studying ubiquitin receptors by NMR. Methods Mol Biol 832:279–303. https://doi.org/10.1007/978-1-61779-474-2_20
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