Molecular tectonics V: Molecular recognition in the formation of molecular networks based on hydrogen bonding and electrostatic interactions

1997 ◽  
Vol 38 (11) ◽  
pp. 1933-1936 ◽  
Author(s):  
Olivier Félix ◽  
Mir Wais Hosseini ◽  
AndréDe Cian ◽  
Jean Fischer
1997 ◽  
Vol 38 (10) ◽  
pp. 1755-1758 ◽  
Author(s):  
Olivier Félix ◽  
Mir Wais Hosseini ◽  
André De Cian ◽  
Jean Fischer

2001 ◽  
Vol 13 (5) ◽  
pp. 619-625 ◽  
Author(s):  
Alex Fragoso ◽  
Roberto Cao ◽  
Alicia Díz ◽  
Ileana Sånchez ◽  
Leticia Sånchez

CrystEngComm ◽  
2015 ◽  
Vol 17 (20) ◽  
pp. 3768-3771 ◽  
Author(s):  
Antonio Bauzá ◽  
Antonio Frontera ◽  
Tiddo J. Mooibroek ◽  
Jan Reedijk

A CSD analysis and DFT study reveal that the nitrogen lone-pair in [N(PPh3)2]+ is partially intact and involved in intramolecular hydrogen bonding.


1993 ◽  
Vol 115 (1) ◽  
pp. 369-370 ◽  
Author(s):  
Erkang Fan ◽  
Scott A. Van Arman ◽  
Scott Kincaid ◽  
Andrew D. Hamilton

2020 ◽  
Author(s):  
Matthew J. Henley ◽  
Brian M. Linhares ◽  
Brittany S. Morgan ◽  
Tomasz Cierpicki ◽  
Carol A. Fierke ◽  
...  

AbstractA key functional event in eukaryotic gene activation is the formation of dynamic protein-protein interaction networks between transcriptional activators and transcriptional coactivators. Seemingly incongruent with the tight regulation of transcription, many biochemical and biophysical studies suggest that activators use nonspecific hydrophobic and/or electrostatic interactions to bind to coactivators, with few if any specific contacts. Here a mechanistic dissection of a set of representative dynamic activator•coactivator complexes, comprised of the ETV/PEA3 family of activators and the coactivator Med25, reveals a different molecular recognition model. The data demonstrate that small sequence variations within an activator family significantly redistribute the conformational ensemble of the complex while not affecting overall affinity, and distal residues within the activator—not often considered as contributing to binding—play a key role in mediating conformational redistribution. The ETV/PEA3•Med25 ensembles are directed by specific contacts between the disordered activator and the Med25 interface, which is facilitated by structural shifts of the coactivator binding surface. Taken together, these data highlight the critical role coactivator plasticity plays in recognition of disordered activators, and indicates that molecular recognition models of disordered proteins must consider the ability of the binding partners to mediate specificity.


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