In-solution structure and oligomerization of human histone deacetylase 6-an integrative approach

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F23%3A00568950" target="_blank" >RIV/86652036:_____/23:00568950 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/23:10448256
Result on the web
<a href="https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.16616" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/10.1111/febs.16616</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/febs.16616" target="_blank" >10.1111/febs.16616</a>

Result language
angličtina
Original language name
In-solution structure and oligomerization of human histone deacetylase 6-an integrative approach
Original language description
Human histone deacetylase 6 (HDAC6) is a structurally unique, multidomain protein implicated in a variety of physiological processes including cytoskeletal remodelling and the maintenance of cellular homeostasis. 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 modelling. 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. Furthermore, HDAC6 forms dimers/higher oligomers in a concentration-dependent manner, and its oligomerization is mediated via the positively charged N-terminal microtubule-binding domain. Our findings provide the first insights into the structure of full-length human HDAC6 and can be used as a basis for further research into structure function and physiological studies of this unique deacetylase.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10608 - Biochemistry and molecular biology

Project
<a href="/en/project/GA21-31806S" target="_blank" >GA21-31806S: Modulation of structural and functional properties of the HSP90 chaperone machinery by reversible acetylation</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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