Sandbox Reserved 431: Difference between revisions

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==Overall Structure==

Cytochrome P450 is an <scene name='48/483888/Cytochrome_p450_dimer/1'>asymmetric dimer</scene>, which means the protein is made of two subunits that are structurally very similar to one another, but not identical. Each dimeric subunit contain 12 α-helices (labeled A-L) along with some β-sheets that are localized to one side of the molecule. Helices F and G from each of the units form the dimer interface of cytochrome P450, and are involved in the formation of the active site. This dimeric interface of the protein is stabilized by <scene name='48/483888/Cytochrome_p450_interface/1'>hydrogen bonding interactions</scene> between residues from the G helix of one the units with residues located on the the F helix of the second unit, and vice versa. Two molecules of 2-hydroxypropyl-β-cyclodextrin are also found near the dimer interface. The cyclodextrins are believed to help further stabilize the protein, and also shield the hydrophobic ~~parts~~ of the F ~~and~~ G ~~helices of each subunit~~ from the solvent by <scene name='48/483888/Cytochrome_p450_cyclodextrins/1'>encapsulating the Phe240 residue within its cavity</scene>. Cytochrome P450 has an apparent mass of ~120 kDa.

Cytochrome P450 is an <scene name='48/483888/Cytochrome_p450_dimer/1'>asymmetric dimer</scene>, which means the protein is made of two subunits that are structurally very similar to one another, but not identical. Each dimeric subunit contain 12 α-helices (labeled A-L) along with some β-sheets that are localized to one side of the molecule. Helices F and G from each of the units form the dimer interface of cytochrome P450, and are involved in the formation of the active site. This dimeric interface of the protein is stabilized by <scene name='48/483888/Cytochrome_p450_interface/1'>hydrogen bonding interactions</scene> between residues from the G helix of one the units with residues located on the the F helix of the second unit, and vice versa. Two molecules of 2-hydroxypropyl-β-cyclodextrin are also found near the dimer interface. The cyclodextrins are believed to help further stabilize the protein, and also shield the hydrophobic part of the F-G helix transition loop from the solvent by <scene name='48/483888/Cytochrome_p450_cyclodextrins/1'>encapsulating the Phe240 residue within its cavity</scene>. Cytochrome P450 has an apparent mass of ~120 kDa.

==Binding Interactions==

Sandbox Reserved 431: Difference between revisions

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 ==Overall Structure==
-Cytochrome P450 is an <scene name='48/483888/Cytochrome_p450_dimer/1'>asymmetric dimer</scene>, which means the protein is made of two subunits that are structurally very similar to one another, but not identical. Each dimeric subunit contain 12 α-helices (labeled A-L) along with some β-sheets that are localized to one side of the molecule. Helices F and G from each of the units form the dimer interface of cytochrome P450, and are involved in the formation of the active site. This dimeric interface of the protein is stabilized by <scene name='48/483888/Cytochrome_p450_interface/1'>hydrogen bonding interactions</scene> between residues from the G helix of one the units with residues located on the the F helix of the second unit, and vice versa. Two molecules of 2-hydroxypropyl-β-cyclodextrin are also found near the dimer interface. The cyclodextrins are believed to help further stabilize the protein, and also shield the hydrophobic parts of the F and G helices of each subunit from the solvent by <scene name='48/483888/Cytochrome_p450_cyclodextrins/1'>encapsulating the Phe240 residue within its cavity</scene>. Cytochrome P450 has an apparent mass of ~120 kDa.
+Cytochrome P450 is an <scene name='48/483888/Cytochrome_p450_dimer/1'>asymmetric dimer</scene>, which means the protein is made of two subunits that are structurally very similar to one another, but not identical. Each dimeric subunit contain 12 α-helices (labeled A-L) along with some β-sheets that are localized to one side of the molecule. Helices F and G from each of the units form the dimer interface of cytochrome P450, and are involved in the formation of the active site. This dimeric interface of the protein is stabilized by <scene name='48/483888/Cytochrome_p450_interface/1'>hydrogen bonding interactions</scene> between residues from the G helix of one the units with residues located on the the F helix of the second unit, and vice versa. Two molecules of 2-hydroxypropyl-β-cyclodextrin are also found near the dimer interface. The cyclodextrins are believed to help further stabilize the protein, and also shield the hydrophobic part of the F-G helix transition loop from the solvent by <scene name='48/483888/Cytochrome_p450_cyclodextrins/1'>encapsulating the Phe240 residue within its cavity</scene>. Cytochrome P450 has an apparent mass of ~120 kDa.
 ==Binding Interactions==