High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2).

@article{Shieh2008HighRC,
  title={High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2).},
  author={Huey-Sheng Shieh and Karl J Mathis and Jennifer M. Williams and Robert L. Hills and Joe F Wiese and Timothy E. Benson and James R. Kiefer and Margaret H Marino and Jeffery N Carroll and Joseph W. Leone and A M Malfait and Elizabeth C Arner and Micky D. Tortorella and Alfredo G. Tomasselli},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 3},
  pages={1501-7}
}
Aggrecanase-2 (a disintegrin and metalloproteinase with thrombospondin motifs-5 (ADAMTS-5)), a member of the ADAMTS protein family, is critically involved in arthritic diseases because of its direct role in cleaving the cartilage component aggrecan. The catalytic domain of aggrecanase-2 has been refolded, purified, and crystallized, and its three-dimensional structure determined to 1.4A resolution in the presence of an inhibitor. A high resolution structure of an ADAMTS/aggrecanase protein… CONTINUE READING