The three-dimensional high resolution structure of human interferon α-2a determined by heteronuclear NMR spectroscopy in solution

1997 ◽  
Vol 274 (4) ◽  
pp. 661-675 ◽  
Author(s):  
Werner Klaus ◽  
Bernard Gsell ◽  
Alexander M. Labhardt ◽  
Beat Wipf ◽  
Hans Senn
Keyword(s):  
Nmr Spectroscopy ◽  
High Resolution ◽  
Heteronuclear Nmr ◽  
Three Dimensional ◽  
Human Interferon ◽  
Interferon Α ◽  
Heteronuclear Nmr Spectroscopy ◽  
High Resolution Structure ◽  
Human Interferon Α ◽  
Resolution Structure

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

2007 ◽  
Vol 283 (3) ◽  
pp. 1501-1507 ◽  
Author(s):  
Huey-Sheng Shieh ◽  
Karl J. Mathis ◽  
Jennifer M. Williams ◽  
Robert L. Hills ◽  
Joe F. Wiese ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Catalytic Domain ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Direct Role ◽  
Three Dimensional Structure ◽  
High Resolution Structure ◽  
A Disintegrin And Metalloproteinase ◽  
Resolution Structure

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 1.4Å 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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