Crystallization and preliminary X-ray study of the cathepsin B complexed with CA074, a selective inhibitor.
Cathepsin B from bovine spleen has been purified and crystallized as a complex with a specific inhibitor CA074 [N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L- isoleucyl-L-proline], using the hanging-drop method. The complex crystals obtained from 50 mM-citrate buffer (pH 3.5) belong to the tetragonal space group P4(1) (or P4(3)) with a = 73.06 A and c = 141.59 A, and diffract beyond 2.2 A resolution. There are two complex molecules per asymmetric unit giving a packing density of 3.37 A3/Da and indicating a high solvent content of 63.5%.
Yamamoto
A
A
Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, Japan.
Kaji
T
T
Tomoo
K
K
Ishida
T
T
Inoue
M
M
Murata
M
M
Kitamura
K
K
D000818:Animals; D002401:Cathepsin B / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D003460:Crystallization; D004151:Dipeptides / Q000737:chemistry* / Q000378:metabolism; D046911:Macromolecular Substances; D008956:Models, Chemical; D014961:X-Ray Diffraction
D004151:Dipeptides; D046911:Macromolecular Substances; C068250:N-(3-propylcarbamoyloxirane-2-carbonyl)-isoleucyl-proline; D002401:Cathepsin B