High Resolution Crystal Structure of the Catalytic Domain of ADAMTS-5 (Aggrecanase-2)
Copyright policy )High Resolution Crystal Structure of the Catalytic Domain of ADAMTS-5 (Aggrecanase-2)
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.
- Pfizer (United States) United States
Models, Molecular, Tissue Inhibitor of Metalloproteinase-3, Protein Folding, Molecular Sequence Data, Temperature, Crystallography, X-Ray, Protein Structure, Secondary, ADAM Proteins, Catalytic Domain, Enzyme Stability, Humans, ADAMTS5 Protein, Amino Acid Sequence, Enzyme Inhibitors
Models, Molecular, Tissue Inhibitor of Metalloproteinase-3, Protein Folding, Molecular Sequence Data, Temperature, Crystallography, X-Ray, Protein Structure, Secondary, ADAM Proteins, Catalytic Domain, Enzyme Stability, Humans, ADAMTS5 Protein, Amino Acid Sequence, Enzyme Inhibitors
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).71 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 1%
Citations provided by BIP!Popularity provided by BIP!