User:Davion Murray/Sandbox1: Difference between revisions
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==Binding site/Ligands== | ==Binding site/Ligands== | ||
The AAA+ ATPase and protease domains of each polypeptide interacts with the substrate proteins in an open/close spiral staircase conformation (3). There are six active sites for proteolytic function inside the chamber made by the conformation. The six long helix regions protrude from the ring overlapping with three long helix regions to make a triangular shaped region. This region positions the six N-terminus domains to surround a central tri-tyrosine pore where substrate entry can occur. These N-terminus domains are flexible and are often thought to be involved with mediating substrate recognition (1). | The AAA+ ATPase and protease domains of each polypeptide interacts with the substrate proteins in an open/close spiral staircase conformation (3). There are six active sites for proteolytic function inside the chamber made by the conformation. The six long helix regions protrude from the ring overlapping with three long helix regions to make a triangular shaped region. This region positions the six N-terminus domains to surround a central tri-tyrosine pore where substrate entry can occur. These N-terminus domains are flexible and are often thought to be involved with mediating substrate recognition (1). In this assembly the <scene name='11/1106429/Lara_binding_sites/1'>LarA C-terminal His89 residue</scene> acts a binding site to C-terminal region of Lon NTDs (aa 197-205)(1) | ||
==Current Research== | ==Current Research== | ||
