Author: Ramasubramanian Sundaramoorthy; Amanda L. Hughes; Hassane El-Mkami; David Norman; Tom Owen-Hughes
Title: Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome Document date: 2018_3_30
ID: ct2zhauz_6
Snippet: Yeast Chd1 serves as a useful paradigm in that it functions predominantly as a single polypetide. In addition, the catalytic core of the enzyme has been crystallised in association with the adjacent tandem chromodomains (Hauk et al., 2010) . Similarly the C-terminal region of the protein has been crystalized revealing that this region includes SANT and SLIDE domains that comprise the DNA binding domain (DNABD) (Ryan et al., 2011b; Sharma et al., .....
Document: Yeast Chd1 serves as a useful paradigm in that it functions predominantly as a single polypetide. In addition, the catalytic core of the enzyme has been crystallised in association with the adjacent tandem chromodomains (Hauk et al., 2010) . Similarly the C-terminal region of the protein has been crystalized revealing that this region includes SANT and SLIDE domains that comprise the DNA binding domain (DNABD) (Ryan et al., 2011b; Sharma et al., 2011) and are also present in ISWI proteins (Grune et al., 2003) . Chd1 enzyme engages nucleosomes in a conformation in which the SANT and SLIDE domains bind linker DNA, while the ATPase domains engage DNA at super helical location (SHL) 2 (Nodelman et al., 2017; Sundaramoorthy et al., 2017) .
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