Table 1.

Summary of characteristics, function, and representative structures of molecular chaperone

Family	Characteristics	Function	PDB ID
Small HSPs (HSPB1~HSPB10)	ATP-independent	Prevent proteins aggregation; Sequestrate misfolded proteins	4MJH, 5LUM, 6F2R 6BP9, 6DV5, 3J07, 6T1R
HSP40 (DnaJA/B/C)	Contain J domain	HSP70 co-chaperone; Accelerate ATP hydrolysis	1HDJ, 2CTQ, 2CTR 2M6Y, 4WB7, 7NDX
HSP60	ATP-dependent	Protein foldase; Prevent proteins aggregation	1GR5, 4PJ1 6MRC, 7AZP, 8G7O
HSP70 (HSP70i, HSC70, GRP75, GRP78)	ATP-dependent	Work as holdase and foldase; Promote polypeptides folding	1ATR, 1HJO, 1XQS, 2LMG 4JNE, 4PO2, 4KBO, 5EXW
HSP90 (HSP90α, HSP90β, GRP94, TRAP1)	ATP-dependent	Promote clients folding; Refold misfolded proteins; Help clients PTMs	2K5B, 1AH6, 1QYE, 1US7 1HK7, 1USV, 2CG9, 2O1V 4J0B, 4O04, 6N8Y, 6XG6, 7RY0, 8X2R, 5FWP, 7L7I, 7KW7, 7KRJ, 7Z38, 7ZR5, 8H77, 8GFT, 8FX4, 8QMO
HSP100 (ClpA/B/C/X)	ATP-dependent	Solublize proteins aggregates; Degradate misfolded proteins	1JBK, 1R6B, 3PXG 6W21, 6SFW
Large HSPs (HSP110, CRP170)	HSP70 superfamily	Co-chaperone of HSP70; Promote ATP-ADP exchange	2QXL, 3C7N, 6GFA

Data source: RCSB Protein Data Bank (https://www.rcsb.org/). If a same structure was released on both RCSB Protein Data Bank, only PDB ID was provided for space saving. Data were last updated on July 25th, 2024