Cargando…
Unique SMYD5 Structure Revealed by AlphaFold Correlates with Its Functional Divergence
SMYD5 belongs to a special class of protein lysine methyltransferases with an MYND (Myeloid-Nervy-DEAF1) domain inserted into a SET (Suppressor of variegation, Enhancer of Zeste, Trithorax) domain. Despite recent advances in its functional characterization, the lack of the crystal structure has hind...
Autores principales: | Zhang, Yingxue, Alshammari, Eid, Sobota, Jacob, Yang, Alexander, Li, Chunying, Yang, Zhe |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9221539/ https://www.ncbi.nlm.nih.gov/pubmed/35740908 http://dx.doi.org/10.3390/biom12060783 |
Ejemplares similares
-
AlphaFold and the future of structural biology
por: Read, Randy J., et al.
Publicado: (2023) -
Applying and improving AlphaFold at CASP14
por: Jumper, John, et al.
Publicado: (2021) -
AlphaFold, Artificial
Intelligence (AI), and Allostery
por: Nussinov, Ruth, et al.
Publicado: (2022) -
Using AlphaFold Predictions in Viral Research
por: Gutnik, Daria, et al.
Publicado: (2023) -
Folding the unfoldable: using AlphaFold to explore spurious
proteins
por: Monzon, Vivian, et al.
Publicado: (2022)