Fig. 6
From: Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin
UNC-45 chaperone function in folding the myosin head domain. Fully functional myosin can be obtained by co-expression with its cognate chaperone UNC-45 in insect cells. UNC-45’s ability to support myosin folding strongly depends on the flexibility of its UCS domain, the functionality of the myosin-binding canyon and its oligomerization properties. UNC-45 ts-mutations limit this conformational flexibility and therefore interfere with myosin binding and chaperone activity
