ArticleThe Journal of biological chemistry2015
RWD Domain as an E2 (Ubc9)-Interaction Module.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Systematic identification of germ granule proteins reveals specialized roles in RNAi and small RNA inheritance.Genes & development · 2026Article
- Emerging Role of GCN1 in Disease and Homeostasis.International journal of molecular sciences · 2024Review
- Updated protein domain annotation of the PARP protein family sheds new light on biological function.Nucleic acids research · 2023Article
- Genetic risk of osteoarthritis operates during human skeletogenesis.Human molecular genetics · 2023Article
- Association of SUMOylation Pathway Genes With Stroke in a Genome-Wide Association Study in India.Neurology · 2021Article
- Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.Chemical reviews · 2018Review
- A framework for exhaustively mapping functional missense variants.Molecular systems biology · 2017Article
- Molecular mechanism of K65 acetylation-induced attenuation of Ubc9 and the NDSM interaction.Scientific reports · 2017Article
- Assessing predictions of fitness effects of missense mutations in SUMO-conjugating enzyme UBE2I.Human mutation · 2017Article
- Article
- Observation of an E2 (Ubc9)-homodimer by crystallography.Data in brief · 2016Article
- Is Transthyretin a Regulator of Ubc9 SUMOylation?PloS one · 2016Article
- Function and Structure of the RWD Domain.The Journal of biological chemistry · 2015Article
- Reply to Function and Structure of the RWD Domain.The Journal of biological chemistry · 2015Article
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9 authors.
Funding
Abstract
An RWD domain is a well conserved domain found through bioinformatic analysis of the human proteome sequence; however, its function has been unknown. Ubiquitin-like modifications require the catalysis of three enzymes generally known as E1, E2, and E3. We solved the crystal structure of the E2 for the small ubiquitin-like modifiers (SUMO) in complex with an RWD domain and confirmed the structure using solution NMR analysis. The binding surface of RWD on Ubc9 is located near the N terminus of Ubc9 that is known to be involved in noncovalent binding of the proteins in the conjugation machinery, including a domain of E1, SUMO, and an E3 ligase. NMR data indicate that the RWD domain does not bind to SUMO and E1. The interaction between RWD and Ubc9 has a Kd of 32 ± 4 μM. Consistent with the structure and binding affinity and in contrast to a previous report, the RWD domain and RWDD3 have minimal effects on global SUMOylation. The structural and biochemical information presented here forms the basis for further investigation of the functions of RWD-containing proteins.
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