Such efforts have been directed at improving binding affinity of existing interfaces as well as changing binding specificity.
Primary binding interfaces A and B, as well as both dimerization interfaces, appear to be only modestly conserved, indicating that flagellin binding probably differs in fish and amniotes.
However, these structures did not define the binding interfaces of the evolutionarily conserved nuclear actin and actin-related proteins (Arps) of INO80 or provide insights into their functional properties10,11,12,13.
Here we define the nucleosome binding interfaces and functions of the evolutionarily conserved Arps in the yeast INO80 chromatin remodeling complex.
This β-Gal binding site is conserved among all BV, NV, FUV and TCH with known crystal structures (Bu et al., 2008; Choi et al., 2008; Kubota et al., 2012; Shanker et al., 2014) and thus may be defined as the central binding pocket (CBP) of GI HBGA binding interfaces, because it plays the central role in GI NoV-HBGA interactions, as proposed previously (Tan and Jiang, 2014).
Our characterisation of the binding interface also allowed us to define a consensus-binding site (PRxxPxP) for the CPAP TCP domain in STIL that is conserved across metazoa.
Solid lines over the alignment indicate protein domains as defined previously for P. abyssi NucS11 (black, DNA-binding; grey, nuclease).
Nuclear magnetic resonance titration maps the binding interfaces between UBZ and ubiquitin to the alpha-helix of the UBZ domain and the canonical hydrophobic surface of ubiquitin defined by residues L8, I44 and V70.
In fact, different replacements of amino acids in the binding interfaces of both GI and GII NoVs are often seen, which serve as examples of some amino acids are replaceable in functional HBGA binding interfaces.
In this paper, we focus on the small elements of user interfaces that are defined as interface signs.
