User:Davion Murray/Sandbox1: Difference between revisions

While the N-terminus domain of Lon has been suggested to be involved with substrate recognition there aren’t many substrates bound structures available to illustrate its role. Current research is being done to structurally illustrate through bound substrate-protein complexes the N-terminal domains regulatory function (1,4). Proteases recognize their substrates by short sequence tags called degrons that are located on the termini of proteins (4.) However, for efficient substrate recognition for protease activity requires adapters and allosteric regulators are needed (4).  One of these is LarA a heat shock protein that accumulates at the onset of proteoxic stress (4). Crystallographic evidence has shown that LarA binds to a conserved groove in the N-terminal domain through an aromatic residue on its C-terminal degron (1). Evidence also shows that this binding exposes the hydrophobic core of LarA. This core can bind a leucine residue and promote local protein unfolding (1). Research on LarA indicates its regulatory function withing the Lon protease complex (1,4).