Binding Mode and Transcriptional Activation Potential of High Affinity Ligands for the CBP KIX Domain

2005 ◽  
Vol 127 (13) ◽  
pp. 4649-4658 ◽  
Author(s):  
Heather M. Volkman ◽  
Stacey E. Rutledge ◽  
Alanna Schepartz
Keyword(s):  
Transcriptional Activation ◽  
Binding Mode ◽  
Affinity Ligands ◽  
High Affinity ◽  
Activation Potential ◽  
Kix Domain

scholarly journals Molecular Recognition of Protein Surfaces:  High Affinity Ligands for the CBP KIX Domain

2003 ◽  
Vol 125 (47) ◽  
pp. 14336-14347 ◽  
Author(s):  
Stacey E. Rutledge ◽  
Heather M. Volkman ◽  
Alanna Schepartz
Keyword(s):  
Molecular Recognition ◽  
Protein Surfaces ◽  
Affinity Ligands ◽  
High Affinity ◽  
Kix Domain

scholarly journals Tripodal, Squaramide-Based Ion Pair Receptor for Effective Extraction of Sulfate Salt

Molecules ◽  
2021 ◽  
Vol 26 (9) ◽  
pp. 2751
Author(s):  
Damian Jagleniec ◽  
Marcin Wilczek ◽  
Jan Romański
Keyword(s):  
Ion Pairs ◽  
Binding Mode ◽  
Selective Extraction ◽  
Ion Pair ◽  
Hofmeister Series ◽  
Sulfate Salt ◽  
Lower Affinity ◽  
High Affinity ◽  
Binding Domains ◽  
Hydrated Sulfate

Combining three features—the high affinity of squaramides toward anions, cooperation in ion pair binding and preorganization of the binding domains in the tripodal platform—led to the effective receptor 2. The lack of at least one of these key elements in the structures of reference receptors 3 and 4 caused a lower affinity towards ion pairs. Receptor 2 was found to form an intramolecular network in wet chloroform, which changed into inorganic–organic associates after contact with ions and allowed salts to be extracted from an aqueous to an organic phase. The disparity in the binding mode of 2 with sulfates and with other monovalent anions led to the selective extraction of extremely hydrated sulfate anions in the presence of more lipophilic salts, thus overcoming the Hofmeister series.

scholarly journals Spanning the gap: unraveling RSC dynamics in vivo

2021 ◽  
Author(s):  
Heinz Neumann ◽  
Bryan J. Wilkins
Keyword(s):  
Cell Cycle ◽  
Posttranslational Modifications ◽  
Transcriptional Activation ◽  
Binding Mode ◽  
Binding Modes ◽  
Binding Domains ◽  
Binding Interface ◽  
The Many ◽  
And Function

AbstractMultiple reports over the past 2 years have provided the first complete structural analyses for the essential yeast chromatin remodeler, RSC, providing elaborate molecular details for its engagement with the nucleosome. However, there still remain gaps in resolution, particularly within the many RSC subunits that harbor histone binding domains.Solving contacts at these interfaces is crucial because they are regulated by posttranslational modifications that control remodeler binding modes and function. Modifications are dynamic in nature often corresponding to transcriptional activation states and cell cycle stage, highlighting not only a need for enriched spatial resolution but also temporal understanding of remodeler engagement with the nucleosome. Our recent work sheds light on some of those gaps by exploring the binding interface between the RSC catalytic motor protein, Sth1, and the nucleosome, in the living nucleus. Using genetically encoded photo-activatable amino acids incorporated into histones of living yeast we are able to monitor the nucleosomal binding of RSC, emphasizing the regulatory roles of histone modifications in a spatiotemporal manner. We observe that RSC prefers to bind H2B SUMOylated nucleosomes in vivo and interacts with neighboring nucleosomes via H3K14ac. Additionally, we establish that RSC is constitutively bound to the nucleosome and is not ejected during mitotic chromatin compaction but alters its binding mode as it progresses through the cell cycle. Our data offer a renewed perspective on RSC mechanics under true physiological conditions.

Purification of bacterial virulence factor pertactin using high affinity ligands

2020 ◽  
Vol 164 ◽  
pp. 107760
Author(s):  
Umatheny Umatheva ◽  
Braden Sweeting ◽  
Léo Sauvaget ◽  
Nerissa Dela Rosa ◽  
John Riley ◽  
...  
Keyword(s):  
Virulence Factor ◽  
Bacterial Virulence ◽  
Affinity Ligands ◽  
High Affinity ◽  
Bacterial Virulence Factor
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