Chaperones: Difference between revisions

Structurally, <scene name='59/591341/Structural_organization/2'>Hsp70</scene> have a N-terminal <scene name='59/591341/Nbd_hsp70/7'>ATPase domain</scene> followed by a <scene name='59/591341/Sbd_of_dnak1/2'>substrate binding domain</scene> with elongated C-terminal. These domains allosterically regulate the hsp70 functioning. <scene name='59/591341/4jn4/2'>4JN4</scene> is a representative example of a chaperone system in complex with ADP. In the 2D figure given below, panel A indicates the various folded (green) and unfolded (red)regions in Hsp70. Panel B shows the structural organization of Hsp 70 indicating its various domains. ATP binding and hydrolysis regulates the affinity for substrate proteins which thereafter enhances ATP hydrolysis.