Solution structure of the zinc finger domain of human RNF144A ubiquitin ligase.
E3 enzyme
NMR structure
RING finger
RNF144A
artificial RING finger
ubiquitination
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
08 2020
08 2020
Historique:
received:
06
03
2020
revised:
12
06
2020
accepted:
13
06
2020
pubmed:
20
6
2020
medline:
16
1
2021
entrez:
20
6
2020
Statut:
ppublish
Résumé
RNF144A is involved in protein ubiquitination and functions as an ubiquitin-protein ligase (E3) via its RING finger domain (RNF144A RING). RNF144A is associated with degradation of heat-shock protein family A member 2 (HSPA2), which leads to the suppression of breast cancer cell proliferation. In this study, the solution structure of RNF144A RING was determined using nuclear magnetic resonance. Moreover, using a metallochromic indicator, we spectrophotometrically determined the stoichiometry of zinc ions and elucidated that RNF144A RING binds two zinc atoms. This structural analysis provided the position and range of the active site of RNF144A RING at the atomic level, which contributes to the creation of artificial RING fingers having the specific ubiquitin-conjugating enzyme (E2)-binding capability.
Identifiants
pubmed: 32557973
doi: 10.1002/pro.3903
pmc: PMC7380669
doi:
Substances chimiques
Carrier Proteins
0
RNF144A protein, human
EC 2.3.2.27
Ubiquitin-Protein Ligases
EC 2.3.2.27
Zinc
J41CSQ7QDS
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1836-1842Informations de copyright
© 2020 The Protein Society.
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