Sandbox Reserved 1125: Difference between revisions
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This pocket is delimited by the Leu193, Val194, His197, Leu214, Tyr216, Tyr219, Ala220 and Arg222 residues.<ref>PMID:17275314</ref>. | This pocket is delimited by the Leu193, Val194, His197, Leu214, Tyr216, Tyr219, Ala220 and Arg222 residues.<ref>PMID:17275314</ref>. | ||
Moreover, this pocket is rich in hydrophobic amino acids, what is suitable for binding to the substrates of MMP-8. | Moreover, this pocket is rich in hydrophobic amino acids, what is suitable for binding to the substrates of MMP-8. | ||
[[Image:CA_pocket_interaction.gif | thumb|CA996 pocket interaction]] | [[Image:CA_pocket_interaction.gif | thumb|CA996 pocket interaction]] | ||
==== Ca2+ interactions ==== | ==== Ca2+ interactions ==== | ||
This enzyme binds 3 Ca ions, 2 of them in the catalytic domain, which are packed against the top of the beta sheet and have mostly a structural function, stabilizing the catalytic domain.<ref name="X-ray"/> | This enzyme binds 3 Ca ions, 2 of them in the catalytic domain, which are packed against the top of the beta sheet and have mostly a structural function, stabilizing the catalytic domain.<ref name="X-ray"/> | ||
The residues involved in the Ca996 interactions (coordinate bonds) are <scene name='71/719866/Ca2_interactions/3'>two Gly residues (169 and 171) next to two Asp residues (137 and 173)</scene>. | The residues involved in the Ca996 interactions (coordinate bonds) are <scene name='71/719866/Ca2_interactions/3'>two Gly residues (169 and 171) next to two Asp residues (137 and 173)</scene>. | ||
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===== Zn998 : the structural zinc ===== | ===== Zn998 : the structural zinc ===== | ||
The residues involved in the Zn998 interactions are <scene name='71/719866/Zn998/2'>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 name="X-ray"/> | The residues involved in the Zn998 interactions are <scene name='71/719866/Zn998/2'>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 name="X-ray"/> | ||
=== Hinge domain === | === Hinge domain === | ||
