1. Differences in Clinical Phenotype among Patients with XP Complementation Group D: 3D Structure and ATP-Docking of XPD In Silico 
Eiji Nakano, Ryusuke Ono, Taro Masaki, Seiji Takeuchi, Yutaka Takaoka, Eiichi Maeda, Chikako Nishigori 
Journal of Investigative Dermatology 
Volume 134, Issue 6, Pages (June 2014)
DOI: /jid
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2. Figure 1
Comparison of three dimensional (3D) structures and electrostatic surface potentials of the XPD protein in silico among wild type and mutants. (a) 3D structures of wild-type and mutant XPD proteins (from the N terminus to the C terminus, blue to red). (b) Electrostatic surface potentials of XPD proteins (from negative potentials to positive potentials, red to blue). (c) Magnification of electrostatic surface potentials of XPD proteins at the ATP-binding site (enclosed by yellow). (d) Results of docking simulation of ATP and XPD proteins. The right panel shows that ATP binds to XPD protein in a previously reported site and orientation. A lower docking score indicates a more energetically stable state.
Journal of Investigative Dermatology  , DOI: ( /jid )
Copyright © 2014 The Society for Investigative Dermatology, Inc Terms and Conditions