Get access

Crystal structure of the cataract-causing P23T γD-crystallin mutant

Authors

  • Fangling Ji,

    1. Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania
    2. School of Life Science and Biotechnology, Dalian University of Technology, Dalian, China
    Search for more papers by this author
  • Leonardus M. I. Koharudin,

    1. Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania
    Search for more papers by this author
  • Jinwon Jung,

    1. Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania
    Search for more papers by this author
  • Angela M. Gronenborn

    Corresponding author
    1. Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania
    • Correspondence to: Angela M. Gronenborn, Department of Structural Biology, University of Pittsburgh School of Medicine, 3501 Fifth Ave., Pittsburgh, PA 15261. E-mail: amg100@pitt.edu

    Search for more papers by this author

ABSTRACT

Up to now, efforts to crystallize the cataract-associated P23T mutant of human γD-crystallin have not been successful. Therefore, insights into the light scattering mechanism of this mutant have been exclusively obtained from solution work. Here we present the first crystal structure of the P23T mutant at 2.5 Å resolution. The protein exhibits essentially the same overall structure as seen for the wild-type protein. Based on our structural data, we confirm that no major conformational changes are caused by the mutation, and that solution phase properties of the mutant appear exclusively associated with cataract formation. Proteins 2013. © 2013 Wiley Periodicals, Inc.

Ancillary