Automated Structure Refinement for a Protein Heterodimer Complex Using Limited EPR Spectroscopic Data and a Rigid-Body Docking Algorithm: A Three-Dimensional Model for an Ankyrin-CDB3 Complex
详细信息 查看全文
- 作者：Sarah J. Edwards ; Christopher W. Moth ; Sunghoon Kim ; Suzanne Brandon ; Zheng Zhou ; Charles E. Cobb ; Eric J. Hustedt ; Albert H. Beth ; Jarrod A. Smith ; Terry P. Lybrand
- 刊名：Journal of Physical Chemistry B
- 出版年：2014
- 出版时间：May 8, 2014
- 年：2014
- 卷：118
- 期：18
- 页码：4717-4726
- 全文大小：534K
- 年卷期：v.118,no.18(May 8, 2014)
- ISSN：1520-5207
文摘
We report here specialized functions incorporated recently in the rigid-body docking software toolkit TagDock to utilize electron paramagnetic resonance derived (EPR-derived) interresidue distance measurements and spin-label accessibility data. The TagDock package extensions include a custom methanethiosulfonate spin label rotamer library to enable explicit, all-atom spin-label side-chain modeling and scripts to evaluate spin-label surface accessibility. These software enhancements enable us to better utilize the biophysical data routinely available from various spin-labeling experiments. To illustrate the power and utility of these tools, we report the refinement of an ankyrin:CDB3 complex model that exhibits much improved agreement with the EPR distance measurements, compared to model structures published previously.