Stabilizing of a Globular Protein by a Highly Complex Water Network: A Molecular Dynamics Simulation Study on Factor Xa
| Autor: | Thomas R. Fox, Sandra Handschuh, Hannes G. Wallnoefer, Klaus R. Liedl |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
chemistry.chemical_classification
Serine protease biology Globular protein Water Plasma protein binding Molecular Dynamics Simulation Surfaces Coatings and Films Molecular dynamics Fibrinolytic Agents chemistry Structural biology Computational chemistry Factor Xa Materials Chemistry biology.protein Biophysics Molecule Physical and Theoretical Chemistry Function (biology) Fibrinolytic agent Protein Binding |
| Zdroj: | The Journal of Physical Chemistry B. 114:7405-7412 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/jp101654g |
| Popis: | The role of water molecules is increasingly attracting attention in structural biology, and many studies have demonstrated their crucial contribution to the stability and function of proteins. Here, we present molecular dynamics studies on factor Xa (fXa) to investigate the effect of water molecules in this serine protease. fXa is a key enzyme in the blood coagulation cascade, and thus, an important target for antithrombotic drugs. A reasonable representation of the structure is crucial for an investigation at the molecular level and, thus, a prerequisite for structure-based drug design. Simulations of well-resolved fXa X-ray structures with different sets of water molecules show the importance of a well-determined water set for the simulation. We discuss implications of different water sets on the structure and dynamics of fXa. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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