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Výsledky projektu Analýza interakcí mezi histon deacetylasou 6 a dyneinem

Výsledky

▼▲Typ výsledku ▼▲Autor celku ▼▲Název celku
(Celkem 4 zázn.)
Shukla Shivam. In‐solution structure and oligomerization of human histone deacetylase 6–an integrative approach.. The FEBS journal, 2022, sv. 290(3), s. 821–836. ISSN 1742-464X. IF 5.622. [Článek v časopise]
Shivam Shukla, Abstract: Human histone deacetylase 6 (HDAC6) is a structurally unique, multidomain protein implicated in a variety of physiological processes. Our current understanding of the HDAC6 structure is limited to isolated domains and a holistic picture of the full-length protein structure, including possible domain interactions, is missing. Here, we used an integrative structural biology approach to build a solution model of HDAC6 by combining experimental data from several orthogonal biophysical techniques complemented by molecular modeling. We show that HDAC6 is best described as a mosaic of folded and intrinsically disordered domains that in-solution adopts an ensemble of conformations without any stable interactions between structured domains. [Jiný výsledek]
Figures, Figures [Jiný výsledek]
Shivam Shukla, Abstract- Histone Deacetylase 6(HDCA6) is a zinc dependent deacetylase that belongs to the class IIb HDAC family. It functions by removing acetyl groups from lysine side chain of target proteins. It’s a multidomain protein comprised of five domains of the total molecular mass of 140 kDa. Given the structural complexity of the wild-type HDAC6 it is a challenging target for X ray crystallography. To glean more structural information on full length human HDAC6, we focused our efforts on creating its integrative structural model by combining several approaches including small-angle X-ray scattering, analytical ultracentrifugation, chemical crosslinking, H/D exchange, native mass spec, and molecular modeling. [Jiný výsledek]