Expression, purification, crystallization and preliminary X-ray diffraction studies of human cathepsin F complexed with an irreversible vinyl sulfone inhibitor.
Cathepsin F is a cysteine protease believed to be involved in the antigen-presenting process of the class II major histocompatibility complex (MHC-II) in macrophages. It has been expressed, purified and crystallized. A complete data set to a resolution of 2.5 A has been collected at room temperature. The Laue group was determined to be orthorhombic, space group P2(1)2(1)2, with unit-cell parameters a = 68.9, b = 104.8, c = 68.5 A.
Ho
Joseph D
JD
Celera Inc, 180 Kimball Way, South San Francisco, CA 94080, USA.
Meltser
Yana
Y
Buggy
Joseph J
JJ
Palmer
James T
JT
Elrod
Kyle C
KC
Chan
Hedy
H
Mortara
Kyle D
KD
Somoza
John R
JR
D001483:Base Sequence; D056646:Cathepsin F; D002403:Cathepsins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D005285:Fermentation; D006801:Humans; D007700:Kinetics; D011487:Protein Conformation; D013450:Sulfones / Q000037:antagonists & inhibitors* / Q000737:chemistry
D017931:DNA Primers; D013450:Sulfones; C009873:divinyl sulfone; D002403:Cathepsins; C534090:CTSF protein, human; D056646:Cathepsin F