Modeling the antiferromagnetic MnIIMnII system within the protein phosphatase-5 catalytic site
| LEADER | caa a22 4500 | ||
|---|---|---|---|
| 001 | 605510733 | ||
| 003 | CHVBK | ||
| 005 | 20210128100647.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 210128e20150101xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.1007/s00894-014-2556-2 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00894-014-2556-2 | ||
| 245 | 0 | 0 | |a Modeling the antiferromagnetic MnIIMnII system within the protein phosphatase-5 catalytic site |h [Elektronische Daten] |c [E. Salter, R. Honkanen, A. Wierzbicki] |
| 520 | 3 | |a Protein phosphatase-5 (PP5), a novel target for inhibition in a search for new antitumor drugs, contains a homobimetallic MnIIMnII system in its catalytic site. The ground electronic state is an antiferromagnetically-coupled singlet. We report optimizations of a known inhibitor within a 42-residue model of the PP5 catalytic site under several two-level hybrid ONIOM computational models. Using the high-resolution crystal structure of a PP5/inhibitor complex as reference, we compare geometric parameters as the qualities of the "high-level” and "low-level” wavefunctions are successively improved by using the correct antiferromagnetic (AF) singlet state. We find that the UB3LYP AF wavefunction for the high-level region is necessary for experimental fidelity. A closed-shell semi-empirical method (RPM6) can be used for the low-quality part of the hybrid scheme to afford geometries which are qualitatively on par with that obtained using the more time-consuming open-shell UB3LYP AF wavefunction. As the AF state can be elusive for such a large system, the ferromagnetic (F) state can also be used in the low-quality calculations without impacting the geometry. | |
| 540 | |a Springer-Verlag Berlin Heidelberg, 2015 | ||
| 690 | 7 | |a Antiferromagnetic bimetal system |2 nationallicence | |
| 690 | 7 | |a DFT |2 nationallicence | |
| 690 | 7 | |a Enzyme-inhibitor interactions |2 nationallicence | |
| 690 | 7 | |a ONIOM |2 nationallicence | |
| 690 | 7 | |a Protein phosphatase-5 |2 nationallicence | |
| 700 | 1 | |a Salter |D E. |u Department of Chemistry, University of South Alabama, 36688, Mobile, AL, USA |4 aut | |
| 700 | 1 | |a Honkanen |D R. |u Department of Biochemistry & Molecular Biology, University of South Alabama, 36688, Mobile, AL, USA |4 aut | |
| 700 | 1 | |a Wierzbicki |D A. |u Department of Chemistry, University of South Alabama, 36688, Mobile, AL, USA |4 aut | |
| 773 | 0 | |t Journal of Molecular Modeling |d Springer Berlin Heidelberg |g 21/1(2015-01-01), 1-5 |x 1610-2940 |q 21:1<1 |1 2015 |2 21 |o 894 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00894-014-2556-2 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00894-014-2556-2 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Salter |D E. |u Department of Chemistry, University of South Alabama, 36688, Mobile, AL, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Honkanen |D R. |u Department of Biochemistry & Molecular Biology, University of South Alabama, 36688, Mobile, AL, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Wierzbicki |D A. |u Department of Chemistry, University of South Alabama, 36688, Mobile, AL, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Journal of Molecular Modeling |d Springer Berlin Heidelberg |g 21/1(2015-01-01), 1-5 |x 1610-2940 |q 21:1<1 |1 2015 |2 21 |o 894 | ||