3B8Z

High Resolution Crystal Structure of the Catalytic Domain of ADAMTS-5 (Aggrecanase-2)

Summary for 3B8Z

• Entry DOI: 10.2210/pdb3b8z/pdb
• Descriptor: protein ADAMTS-5, ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: alpha/beta, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix : Q9UNA0
• Total number of polymer chains: 2
• Total formula weight: 49330.38

Authors

Shieh, H.-S.,Williams, J.M.,Mathis, K.J.,Tortorella, M.D.,Tomasselli, A. (deposition date: 2007-11-02, release date: 2007-12-11, Last modification date: 2024-10-30)

Primary citation

Shieh, H.S.,Mathis, K.J.,Williams, J.M.,Hills, R.L.,Wiese, J.F.,Benson, T.E.,Kiefer, J.R.,Marino, M.H.,Carroll, J.N.,Leone, J.W.,Malfait, A.M.,Arner, E.C.,Tortorella, M.D.,Tomasselli, A.
High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2).
J.Biol.Chem., 283:1501-1507, 2008

PubMed 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.

PubMed: 17991750
DOI: 10.1074/jbc.M705879200

Experimental method

X-RAY DIFFRACTION (1.4 Å)