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High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2) |
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| Authors: | Shieh Huey-Sheng Mathis Karl J Williams Jennifer M Hills Robert L Wiese Joe F Benson Timothy E Kiefer James R Marino Margaret H Carroll Jeffery N Leone Joseph W Malfait Anne-Marie Arner Elizabeth C Tortorella Micky D Tomasselli Alfredo |
| Affiliation: | Pfizer Global Research and Development, 700 Chesterfield Parkway, Chesterfield, MO 63017, USA. |
| Abstract: | 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 provides an opportunity for the development of therapeutics to treat osteoarthritis. |
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