page_title: Prefoldin
hierarchical_section_title: Prefoldin
caption_attribution_description: English: 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 defraction. The protein contains three subunits of unique polymer chains. This image can be found at http://www.pdb.org/pdb/explore.do?structureId=1FXK, {{PD-USGov}}.
context_page_description: 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.
context_section_description: 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.
caption: This is the crystal structure of an archaeal prefoldin taken from the archaeon 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...)
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