Sandbox 177: Difference between revisions
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==='''Structure'''=== | ==='''Structure'''=== | ||
---- | ---- | ||
<applet load='3es9' size=' | <applet load='3es9' size='275' color='black' frame='true' align='left' scene='Sandbox_177/Cyporplain/2' caption='Figure 1: Highlighting the chains and associated ligands of CYPOR'/> | ||
CYPOR is a complex, multidomain protein composed of three chains (<scene name='Sandbox_177/Cyporchaina/2'>A</scene>, <scene name='Sandbox_177/Cyporchainb/1'>B</scene>, <scene name='Sandbox_177/Cyporchainc/1'>C</scene>). 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> (Fig 1).<ref name="5TSON"/> The three associated binding domains for these ligand types, a connecting domain and a transmembrane anchor make up the important structural elements of CYPOR (Fig 2). | CYPOR is a complex, multidomain protein composed of three chains (<scene name='Sandbox_177/Cyporchaina/2'>A</scene>, <scene name='Sandbox_177/Cyporchainb/1'>B</scene>, <scene name='Sandbox_177/Cyporchainc/1'>C</scene>). 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> (Fig 1).<ref name="5TSON"/> The three associated binding domains for these ligand types, a connecting domain and a transmembrane anchor make up the important structural elements of CYPOR (Fig 2). | ||
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==='''Function'''=== | ==='''Function'''=== | ||
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[[Image:CPR chargepair.gif|thumb|right| | [[Image:CPR chargepair.gif|thumb|right|300px|Figure 2: Electrostatic charge pairing between Cyt P450 and the FMN binding domain induces the interaction between CYPOR and Cyt P450.]] | ||
''In vivo'' CYPOR is believe to alternate between a one and a three electron reduced form. While the 1 electron form is fairly stable, forming a neutral blue semiquinone, it is the hydroquinone, or 3 electron form, that is able to donate electrons to the desired redox partners. | ''In vivo'' CYPOR is believe to alternate between a one and a three electron reduced form. While the 1 electron form is fairly stable, forming a neutral blue semiquinone, it is the hydroquinone, or 3 electron form, that is able to donate electrons to the desired redox partners. | ||
