Chaperones: Difference between revisions

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 == Structural highlights ==
-Structurally, hsp70 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. 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.
+Structurally, hsp70 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. In the 2D figure given below, panel A 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. Panel B predicts the various folded (green) and unfolded (red)regions in Hsp70.
 [[Image:HSP_70.JPG|left|500px|thumb|Structural organization of Hsp70]]
 </StructureSection>