We sought to obtain further evidence for the ligand-binding role of the ASRAH domains based on their domain architectures and predicted operonic associations.
Nannocystin A is a potent antiproliferative cyclodepsipeptide targeting eukaryotic translation elongation factor 1α. To elucidate the binding role of its (2R,3S -epoxide, we designed and synthesized a focused library of 10 nannocystin analogues.
In the kinetoplastid MKPs the presence of LRRs and pseudokinase domains may replace the specific binding role of such domains.
Consistent with these identities, the essential binding roles of three residues (Pro-363, Pro-366, Arg-368, indicated by black boxes of Figure 3D) were previously demonstrated by mutational analyses [ 18].
To confirm the microtubule-binding role of Sec61β in a physiological setting, we monitored the levels of ER stress in C. elegans upon the expression of various Sec61β constructs.
To further investigate the membrane-binding role of native α-Syn on v-vesicle clustering, and to extend our findings to PD, we performed experiments with the three PD-related mutants A30P, E46K, and A53T.
While FPs and deletion mutants of the bottom lobe both suggest that the bottom lobe of the ATD is crucial for antibody binding, the role of the S1 domain is more ambiguous.
It is important to mention that, although the C-terminal sequence harbors a Cdc6 binding region, the role of the N-terminal PR70 sequence prior to residue 439 in Cdc6 binding remained to be determined.
Remarkably, in this case, a reverse transition to a helical secondary structure is observed after binding, highlighting the role of the membrane as a template (partitioning-folding coupling).
Changes in the enzyme structure upon inhibitor binding clarify the role of the mobile β3 β4 loop.
