8d4y

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8d4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d4y OCA], [https://pdbe.org/8d4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d4y RCSB], [https://www.ebi.ac.uk/pdbsum/8d4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d4y ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

CHD4 is an essential, widely conserved ATP-dependent translocase that is also a broad tumour dependency. In common with other SF2-family chromatin remodelling enzymes, it alters chromatin accessibility by repositioning histone octamers. Besides the helicase and adjacent tandem chromodomains and PHD domains, CHD4 features 1000 residues of N- and C-terminal sequence with unknown structure and function. We demonstrate that these regions regulate CHD4 activity through different mechanisms. An N-terminal intrinsically disordered region (IDR) promotes remodelling integrity in a manner that depends on the composition but not sequence of the IDR. The C-terminal region harbours an auto-inhibitory region that contacts the helicase domain. Auto-inhibition is relieved by a previously unrecognized C-terminal SANT-SLIDE domain split by ~150 residues of disordered sequence, most likely by binding of this domain to substrate DNA. Our data shed light on CHD4 regulation and reveal strong mechanistic commonality between CHD family members, as well as with ISWI-family remodellers.

The role of auxiliary domains in modulating CHD4 activity suggests mechanistic commonality between enzyme families.,Zhong Y, Moghaddas Sani H, Paudel BP, Low JKK, Silva APG, Mueller S, Deshpande C, Panjikar S, Reid XJ, Bedward MJ, van Oijen AM, Mackay JP Nat Commun. 2022 Dec 6;13(1):7524. doi: 10.1038/s41467-022-35002-0. PMID:36473839<ref>PMID:36473839</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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