ANAT 261 Study Guide - Midterm Guide: Hsp60, Hsp70, Keyboard Shortcut
16 Mar 2012
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Document Summary
A mutation in a cytosolic protein from f to c results in a protein that does not fold correctly. Why? decrease hydrophobicity results in core of protein not established and thus destabilized structure. Loss of f disrupts binding of proteins with partner and thus disrupts quaternary structure. F is key binding residue for hydrophobic ligand that"s required for folding. Protein able to form non-specific interactions between the c and cellular components. Differentiate between the 3 chaperone families: all are atp dependent, use to control substrate binding and release. Atp-bound states bind substrate for hsp70, but not hsp60 or 90. Targets: hsp70-versatile (short stretches and unfolded proteins), hsp90 (proteins closer to native state). Hsp60 can only target small proteins, usually nearer to the native state. Hsp70 used to fold newly synthesized proteins and proteins being translocated to the er and mitochondria. Hsp90 key mediator of heat shock response (with hsf1) Hsp70 and 90 are used to stabilize hormone receptors.
