Sandbox 36: Difference between revisions
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==Catalytic Inhibitors== | ==Catalytic Inhibitors== | ||
Stefin B acts as a competitive inhibitor to cysteine proteases that binds tightly but reversibly to the papain active site. Stefin inhibitors are characterized by M<sub>r</sub> of about 11,000, no disulfphie bonds and no associated carbohydrates. | Stefin B acts as a competitive inhibitor to cysteine proteases that binds tightly but reversibly to the papain active site. Stefin inhibitors are characterized by M<sub>r</sub> of about 11,000, no disulfphie bonds and no associated carbohydrates. | ||
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There are a small number of <scene name='Sandbox_36/Papain_inhibitor_direct_bond/2'>direct hydrogen bonds</scene> between stefin B and papain, however there are many more polar interactions mediated by <scene name='Sandbox_36/Papain_inhibitor_bridges_inter/1'>solvent bridges</scene>. Thirteen solvent molecules bridge polar residues of the enzyme and inhibitor. Seventeen hydrogen bonds are made with a solvent molecule and stefin. Fourteen of these bridges form a papain contact. The rest of the interactions are largely hydrophobic-- involving apolar <scene name='Sandbox_36/Papain_inhibitor_hydro_inter/2'>Van der Waals interactions</scene>. | There are a small number of <scene name='Sandbox_36/Papain_inhibitor_direct_bond/2'>direct hydrogen bonds</scene> between stefin B and papain, however there are many more polar interactions mediated by <scene name='Sandbox_36/Papain_inhibitor_bridges_inter/1'>solvent bridges</scene>. Thirteen solvent molecules bridge polar residues of the enzyme and inhibitor. Seventeen hydrogen bonds are made with a solvent molecule and stefin. Fourteen of these bridges form a papain contact. The rest of the interactions are largely hydrophobic-- involving apolar <scene name='Sandbox_36/Papain_inhibitor_hydro_inter/2'>Van der Waals interactions</scene>. <ref> http://www.ncbi.nlm.nih.gov/pmc/articles/PMC551902/pdf/emboj00233-0254.pdf </ref> | ||
==References== | |||
<references/> | |||
