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Myeloperoxidase crystal structure

Fiedler TJ, Davey CA, Fenna RE (2000) X-Ray Crystal Structure and Characterization of Halide-Binding Sties of Human Myeloperoxidase at 1.8 A Resolution. J Biol Chem 275 11964... [Pg.490]

Zeng J, Fenna RE (1992) X-ray crystal-structure of canine myeloperoxidase at 3 A resolution. J Mol Biol 226 185-207... [Pg.56]

Crystallography revealed a bound chloride ion at the amino terminus of the helix containing the proximal His336 which can be replaced with bromide. Crystal structures of the human MPO-cyanide, MPO-cyanide-bromide, and MPO-cyanide-thiocyanate have also been determined by Fenna and coworkers to 1.9 A. These results support a model for a single common binding site for halides and thiocyanate as substrates or as inhibitors near the S-meso carbon of the porphyrin ring in myeloperoxidase. [Pg.1949]

Figure 9 Structure of myeloperoxidase (MPO) along with the heme environment as observed in the high-resoiution crystal stmcture. (This figure was generated from coordinates of ICXP deposited in the Protein Data Banlr)... Figure 9 Structure of myeloperoxidase (MPO) along with the heme environment as observed in the high-resoiution crystal stmcture. (This figure was generated from coordinates of ICXP deposited in the Protein Data Banlr)...

See other pages where Myeloperoxidase crystal structure is mentioned: [Pg.194]    [Pg.194]    [Pg.80]    [Pg.372]    [Pg.1948]    [Pg.1947]    [Pg.284]    [Pg.34]   
See also in sourсe #XX -- [ Pg.88 , Pg.89 ]




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