Sandbox Reserved 1125: Difference between revisions

Line 40:

==== Ca2+ ====

[[Image:CA_pocket_interaction.gif | thumb|CA pocket interaction]]This enzyme binds 3 CA ions per subunit.

The residues involved in the Ca interactions are <scene name='71/719866/Ca2_interactions/1'>two Gly residues (169 and 171) next to two Asp residues (137 and 173)</scene>.

The residues involved in the Ca996 interactions are <scene name='71/719866/Ca2_interactions/1'>two Gly residues (169 and 171) next to two Asp residues (137 and 173)</scene>.

<font color='red'>maintain a Zn2+ atom coordinated with three water molecules. One of them is as well bound to the Glu residue thanks to a hydrogen bond. The second Zn2+ atom is not involved in the active site. 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.</font>

==== Zn2+ ====

The Zn ion which is involved in the catalytic activity is the Zn999. In a publication (http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940/?page=2) which studies the catalytic domain of MMP8 thanks to the Pro-Leu-Gly-hydroxylamine inhibitor, this ion is penta-coordinated with: His197, His201 and His207 of MMP8 and with the carbonyl and the hydroxyl oxygen of the hydroxamic acid moiety of the inhibitor.

[[Image:ZN pocket interaction.gif | thumb|ZN pocket interaction]]

The residues involved in the Zn interactions are one Asp residue (149) next to three His residues (147, 162 and 175).

Sandbox Reserved 1125: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 40: / Line 40: @@
 ==== Ca2+ ====
 [[Image:CA_pocket_interaction.gif | thumb|CA pocket interaction]]This enzyme binds 3 CA ions per subunit.
-The residues involved in the Ca interactions are <scene name='71/719866/Ca2_interactions/1'>two Gly residues (169 and 171) next to two Asp residues (137 and 173)</scene>.
+The residues involved in the Ca996 interactions are <scene name='71/719866/Ca2_interactions/1'>two Gly residues (169 and 171) next to two Asp residues (137 and 173)</scene>.
-<font color='red'>maintain a Zn2+ atom coordinated with three water molecules. One of them is as well bound to the Glu residue thanks to a hydrogen bond. The second Zn2+ atom is not involved in the active site. 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.</font>
 ==== Zn2+ ====
+The Zn ion which is involved in the catalytic activity is the Zn999. In a publication (http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940/?page=2) which studies the catalytic domain of MMP8 thanks to the Pro-Leu-Gly-hydroxylamine inhibitor, this ion is penta-coordinated with: His197, His201 and His207 of MMP8 and with the carbonyl and the hydroxyl oxygen of the hydroxamic acid moiety of the inhibitor.
 [[Image:ZN pocket interaction.gif | thumb|ZN pocket interaction]]
 The residues involved in the Zn interactions are one Asp residue (149) next to three His residues (147, 162 and 175).