The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Structural Dynamics of E6AP E3 Ligase HECT Domain and Involvement of a Flexible Hinge Loop in the Ubiquitin Chain Synthesis Mechanism
Open accessPublished version of a preprint
Abstract
Abstract Ubiquitin (Ub) ligases E3 are an important factor in selecting target proteins for ubiquitination and determining the type of polyubiquitin chains on the target proteins. In the HECT (homologous to E6AP C-terminus)-type E3 ligases, the HECT domain is composed of an N-lobe containing the E2-binding site and a C-lobe containing the catalytic Cys residue that forms a thioester bond with Ub. These two lobes are connected by a flexible hinge loop. The large conformational rearrangement of the HECT domain via the flexible hinge loop is essential for HECT-type E3-mediated Ub transfer from E2 to a target protein. However, detailed insights into the structural dynamics of this type of E3 ligases remain unclear. Here, we provide the first direct demonstration of structural dynamics of the E6AP HECT domain using high-speed atomic force microscopy. We also investigated structural dynamics of hinge loop flexibility restricted HECT domain, and we found that flexibility of the E6AP hinge loop has a great impact not only on its structural dynamics but also on the formation of free Ub chains mediated by E3-E3 interactions.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Flagged first, then by citations
Research works printed but not linked: 17
- 10.1073/pnas.72.1.11 · DOI
- 10.1152/physrev.00027.2001 · DOI
- 10.1016/j.molcel.2009.11.010 · DOI
- 10.1073/pnas.92.11.5249-a · DOI
- 10.1126/science.286.5443.1321 · DOI
- 10.1016/j.cell.2009.03.007 · DOI
- 10.1016/j.str.2021.09.006 · DOI
- 10.1016/j.str.2020.04.013 · DOI
- 10.1016/S1097-2765(02)00774-8 · DOI
- 10.1371/journal.pcbi.1008444 · DOI
- 10.1371/journal.pcbi.1009970 · DOI
- 10.1074/jbc.RA119.008374 · DOI
- 10.1074/jbc.M100034200 · DOI
- 10.1038/sj.emboj.7600895 · DOI
- 10.1074/jbc.M117.789479 · DOI
- 10.1074/jbc.M113.517805 · DOI
- 10.1016/j.bbrc.2017.12.076 · DOI
Cited by
Sorted by citations
Amyot, R., Miyashita, O., Wu, X., Takeda, K., Kodera, N., Konno, H., Tama, F., & Flechsig, H. (2025) · ACS Nano · doi:10.1021/acsnano.5c10073 · Cited by 13
Self-citation
Metadata
- Authors
- Takeda, K., Flechsig, H., Muro, I., Amyot, R., Kobayashi, F., Kodera, N., Ando, T., & Konno, H.
- Affiliations
- Kanazawa University (JP)
- Corresponding author
- Konno, Hiroki
- Venue
- Nano Letters
- Publisher
- American Chemical Society (ACS)
- Published
- 2023-12-06
- Volume
- 23
- Issue
- 24
- Pages
- 11940-11948
- ISSN
- 1530-6984 (ISSN-L)
- 1530-6992
- PMC
- PMC10755755
- OpenAlex
- W4389369948
- Cited by
- 13
- References
- 1
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 1 · 2023: 3
- FWCI
- 1.16
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Nano Letters (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Core Research for Evolutional Science and Technology (JPMJCR1762)
- Princess Takamatsu Cancer Research Fund
- Japan Society for the Promotion of Science (25112507, 22KF0153)
- Kanazawa University
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Keywords
- UBE3A, HECT E3 ubiquitin ligase, HECT domain, structural dynamics, ubiquitination, conformational change, high-speed atomic force microscopy
- MeSH terms
- Ubiquitin, Polyubiquitin, Ubiquitin-Protein Ligases, Ubiquitination
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
