Water-mediated biomolecular dynamics and allostery.
J Chem Phys
; 152(24): 240901, 2020 Jun 28.
Article
in En
| MEDLINE
| ID: mdl-32610961
ABSTRACT
Dynamic coupling with water contributes to regulating the functional dynamics of a biomolecule. We discuss protein-water dynamics, with emphasis on water that is partially confined, and the role of protein-confined water dynamics in allosteric regulation. These properties are illustrated with two systems, a homodimeric hemoglobin from Scapharca inaequivalvis (HbI) and an A2A adenosine receptor (A2AAR). For HbI, water-protein interactions, long known to contribute to the thermodynamics of cooperativity, are seen to influence the dynamics of the protein not only around the protein-water interface but also into the core of each globule, where dynamic and entropic changes upon ligand binding are coupled to protein-water contact dynamics. Similarly, hydration waters trapped deep inside the core region of A2AAR enable the formation of an allosteric network made of water-mediated inter-residue contacts. Extending from the ligand binding pocket to the G-protein binding site, this allosteric network plays key roles in regulating the activity of the receptor.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Hemoglobins
/
Water
/
Receptor, Adenosine A2A
Limits:
Animals
Language:
En
Journal:
J Chem Phys
Year:
2020
Type:
Article
Affiliation country:
United States