Characterization, crystallization and preliminary crystallographic analysis of human recombinant cyclooxygenase-2.
Acta Crystallogr D Biol Crystallogr
; 53(Pt 2): 224-6, 1997 Mar 01.
Article
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| ID: mdl-15299964
Purified recombinant membrane apoprotein cyclooxygenase-2 (COX-2) has been reconstituted with heme and characterized. The holoprotein has been crystallized in complex with the selective inhibitor CGP 28238 [6-(2,4-difluorophenoxy)-5- methylsulfonylamino-l-indanone] by the sitting-drop method of vapor diffusion using polyethylene glycol 2000 monomethyl ether as precipitant, in the presence of the nonionic detergent beta-octylglucoside. The crystals are orthorhombic, belonging to the space group P2(1)2(1)2 with cell dimensions a = 209.56, b = 71.28 and c = 93.82 A, and diffract to 2.5 A resolution. The asymmetric unit contains two COX-2 monomers, as confirmed by the molecular replacement solution and in agreement with the dimeric structure of the detergent-solubilized protein found with dynamic light scattering and size-exclusion chromatography. Structural work is in progress.
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01-internacional
Base de datos:
MEDLINE
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Año:
1997
Tipo del documento:
Article
País de afiliación:
Suiza
Pais de publicación:
Estados Unidos