Sandbox Reserved 1125: Difference between revisions
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[[Image:ZN pocket interaction.gif | thumb|ZN999 pocket interaction]] | [[Image:ZN pocket interaction.gif | thumb|ZN999 pocket interaction]] | ||
===== Zn998 : the structural zinc ===== | ===== Zn998 : the structural zinc ===== | ||
The residues involved in the Zn998 interactions are <scene name='71/719866/Zn998/1'>an Asp residue (149) next to three His residues (147, 162 and 175)</scene>. The glutamic acid adjacent to the first histidine is essential for catalysis. It | The residues involved in the Zn998 interactions are <scene name='71/719866/Zn998/1'>an Asp residue (149) next to three His residues (147, 162 and 175)</scene>. The glutamic acid adjacent to the first histidine is essential for catalysis. It should be noted that scientists were unable to exchange or remove this Zinc in their crystals, which is suggesting that there is a tight interaction with MMP-8.<ref>PMID:8137810</ref> | ||
One of them is as well bound to the Glu residue thanks to a hydrogen bond. At first, the Gly 206 residue of the substrate binds the active site thanks to the Zn2+ atom. When it binds it takes the place of unstable water molecules and establishes stabilizing interactions with the active site thanks to its C terminal part. Then, the Ala 182 residue of the enzyme makes a hydrogen bond with the NH group of the substrate: this allows the substrate to enter the cavity of the catalytic site. The rest of the protein is stabilized by 4 hydrogen bonds with the amino acid located in the cavity. | One of them is as well bound to the Glu residue thanks to a hydrogen bond. At first, the Gly 206 residue of the substrate binds the active site thanks to the Zn2+ atom. When it binds it takes the place of unstable water molecules and establishes stabilizing interactions with the active site thanks to its C terminal part. Then, the Ala 182 residue of the enzyme makes a hydrogen bond with the NH group of the substrate: this allows the substrate to enter the cavity of the catalytic site. The rest of the protein is stabilized by 4 hydrogen bonds with the amino acid located in the cavity. | ||
