Ketosteroid Isomerase: Difference between revisions
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===Dimer Interface=== | ===Dimer Interface=== | ||
The biologically active unit of KSI is a 2-fold symmetric dimer in which the two chains are packed together via hydrophobic and electrostatic interactions between the "back faces" of the β-sheets. The curved β-sheets on each of the monomers expose convex faces to each other, forming well-defined interactions. In their NMR structure of KSI, Massiah et al. identified interchain hydrophobic interactions (A), as well, a number of polar residues (B) located within the dimer interface. | The biologically active unit of KSI is a 2-fold symmetric dimer in which the two chains are packed together via hydrophobic and electrostatic interactions between the "back faces" of the β-sheets. The curved β-sheets on each of the monomers expose convex faces to each other, forming well-defined interactions. In their NMR structure of KSI, Massiah et al. identified interchain hydrophobic interactions (A), as well, a number of polar residues (B) located within the dimer interface. | ||
[[Image:dimer_interface.png|thumb|center|1000px|'''Interactions at KSI's dimer interface''' (A) Hydrophobic residues. (B) Hydrophillic residues.]] | [[Image:dimer_interface.png|thumb|center|1000px|'''Interactions at KSI's dimer interface''' (A) Hydrophobic residues. (B) Hydrophillic residues.]] | ||
