Protein folding, misfolding and amyloid

Proteins must fold into the right shape to work, and cells use chaperones such as GroEL and Hsp90 to help, and the proteasome to destroy proteins that fail. When folding goes wrong, some proteins stack into long amyloid fibrils. Fibrils of amyloid-beta, tau and alpha-synuclein are hallmarks of Alzheimer's and Parkinson's disease, and misfolded prion proteins cause mad cow disease.

Open GroEL-GroES chaperonin complex in 3D

21 structures

GroEL-GroES chaperonin complex1AON
A folding chamber that gives a protein a protected space to fold.
GroEL chaperonin1OEL
Hsp90 chaperone in a closed state2CG9
Yeast 20S proteasome1RYP
Human 20S proteasome5LE5
Human 26S proteasome5GJR
Ubiquitin1UBQ
Human prion protein1QLX
HET-s prion in its amyloid form2RNM
Amyloid-beta(1-42) fibril (NMR model)2BEG
Amyloid-beta(1-42) fibril by cryo-EM5OQV
Tau paired helical filament from Alzheimer's disease brain5O3L
Tau filament from chronic traumatic encephalopathy6NWP
Alpha-synuclein fibril by solid-state NMR2N0A
Alpha-synuclein fibril by cryo-EM6A6B
Human transthyretin1F41
Mutant transthyretin can form amyloid deposits in the heart and nerves.
Human tau (AlphaFold)P10636 (AlphaFold)
Human alpha-synuclein (AlphaFold)P37840 (AlphaFold)
Human amyloid-beta precursor protein (AlphaFold)P05067 (AlphaFold)
Human transthyretin (AlphaFold)P02766 (AlphaFold)
Human alpha-1-antitrypsin (AlphaFold)P01009 (AlphaFold)

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