Sandbox 177: Difference between revisions
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<applet load='3es9' size='200' color='black' frame='true' align='left' scene='Sandbox_177/Cyporplain/2' caption='Highlighting the CYPOR associated ligands'/> | <applet load='3es9' size='200' color='black' frame='true' align='left' scene='Sandbox_177/Cyporplain/2' caption='Highlighting the CYPOR associated ligands'/> | ||
CYPOR is a complex, multidomain protein | CYPOR is a complex, multidomain protein composed of three chains (A,B,C). It also has three different types of associated ligands; one <scene name='Sandbox_177/Cyporfmn/2'>FMN</scene>, three <scene name='Sandbox_177/Cyporfad/2'>FAD</scene> and two <scene name='Sandbox_177/Cypornadph/2'>NADPH</scene>.<ref name="5TSON"/> | ||
The N-terminus consists of a single alpha-helix that functions as a transmembrane anchor (~6kDa), holding the protein in the endoplasmic reticulum. The portion of the protein responsible for reducing cytochrome P450 is soluble and ~66kDa.<ref name="5TSON"/> The first 170 residues of the soluble region are very similar to those of flavodoxin, which correlates to the fact that this is the area that binds FMN. The FAD and NADPH binding domain is located in the C-terminal section, and is very similar to the FAD domain in ferredoxin-NADP<sup>+</sup> oxidoreductase both in terms of sequence and structure.<ref name="5TSON"/> | The N-terminus consists of a single alpha-helix that functions as a transmembrane anchor (~6kDa), holding the protein in the endoplasmic reticulum. The portion of the protein responsible for reducing cytochrome P450 is soluble and ~66kDa.<ref name="5TSON"/> The first 170 residues of the soluble region are very similar to those of flavodoxin, which correlates to the fact that this is the area that binds FMN. The FAD and NADPH binding domain is located in the C-terminal section, and is very similar to the FAD domain in ferredoxin-NADP<sup>+</sup> oxidoreductase both in terms of sequence and structure.<ref name="5TSON"/> | ||
