Abstract
The nuclear membrane protein 5-lipoxygenase-activating protein (FLAP) plays an essential role in leukotriene synthesis. Recombinant full-length human FLAP with a C-terminal hexahistidine tag has been expressed and purified from the cytoplasmic membrane of Escherichia coli. Diffraction-quality crystals of FLAP in complex with leukotriene-synthesis inhibitor MK-591 and with an iodinated analogue of MK-591 have been grown using the sitting-drop vapor-diffusion method. The crystals exhibit tetragonal symmetry (P42(1)2) and diffracted to a resolution limit of 4 A.
Publication types
-
Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
-
5-Lipoxygenase-Activating Proteins
-
Carrier Proteins / chemistry*
-
Carrier Proteins / genetics
-
Carrier Proteins / isolation & purification
-
Carrier Proteins / metabolism*
-
Crystallization
-
Crystallography, X-Ray
-
Gene Expression*
-
Humans
-
Leukotrienes / biosynthesis*
-
Membrane Proteins / chemistry*
-
Membrane Proteins / genetics
-
Membrane Proteins / isolation & purification
-
Membrane Proteins / metabolism*
-
Molecular Structure
Substances
-
5-Lipoxygenase-Activating Proteins
-
ALOX5AP protein, human
-
Carrier Proteins
-
Leukotrienes
-
Membrane Proteins