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Communications: Electron polarization critically stabilizes the Mg2+ complex in the catalytic core domain of HIV-1 integrase.
- Source :
- Journal of Chemical Physics; 4/7/2010, Vol. 132 Issue 13, p131101, 4p, 1 Diagram, 2 Graphs
- Publication Year :
- 2010
-
Abstract
- In this paper, we present a detailed dynamics study of the catalytic core domain (CCD) of HIV-1 integrase using both polarized and nonpolarized force fields. The numerical results reveal the critical role of protein polarization in stabilizing Mg<superscript>2+</superscript> coordination complex in CCD. Specifically, when nonpolarized force field is used, a remarkable drift of the Mg<superscript>2+</superscript> complex away from its equilibrium position is observed, which causes the binding site blocked by the Mg<superscript>2+</superscript> complex. In contrast, when polarized force field is employed in MD simulation, HIV-1 integrase CCD structure is stabilized and both the position of the Mg<superscript>2+</superscript> complex and the binding site are well preserved. The detailed analysis shows the transition of α-helix to 3<subscript>10</subscript>-helix adjacent to the catalytic loop (residues 139–147), which correlates with the dislocation of the Mg<superscript>2+</superscript> complex. The current study demonstrates the importance of electronic polarization of protein in stabilizing the metal complex in the catalytic core domain of HIV-1 integrase. [ABSTRACT FROM AUTHOR]
- Subjects :
- POLARIZATION (Nuclear physics)
PROTEINS
HIV
SIMULATION methods & models
EQUILIBRIUM
Subjects
Details
- Language :
- English
- ISSN :
- 00219606
- Volume :
- 132
- Issue :
- 13
- Database :
- Complementary Index
- Journal :
- Journal of Chemical Physics
- Publication Type :
- Academic Journal
- Accession number :
- 49033986
- Full Text :
- https://doi.org/10.1063/1.3360769