Prefoldin
![This is the crystal structure of an archaeal prefoldin taken from the archaea bacteria Methanobacterium thermoautotrophicum. The image was produced by Siegerts, R., Scheufler, C., Moarefi, I. using X-Ray diffraction. The heterohexameric protein complex contains two alpha subunits, and four beta subunits.
(more details...)](/Images/godic/202502/04/Prefoldin_3D_Structure2644.jpg")
Prefoldin is a family of proteins used in protein folding complexes. It is classified as a heterohexameric molecular chaperone in both archaea and eukarya, including humans. A prefoldin molecule works as a transfer protein in conjunction with a molecule of chaperonin to form a chaperone complex and correctly fold other nascent proteins. One of prefoldin's main uses in eukarya is the formation of molecules of actin for use in the eukaryotic cytoskeleton.