Biomaterial Database

Molecular chaperones in cellular protein folding. 1995

F U Hartl, and J Martin

Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.

Protein folding in the cell requires molecular chaperones. The chaperone proteins of the hsp70 and hsp60 (chaperonin) classes stabilize unfolded or partially folded polypeptides, thereby preventing aggregation, and mediate folding to the native state in ATP-dependent reactions. Recent advances include a more detailed understanding of the mechanistic principles of hsp70 and hsp60 action, the solution of the crystal structure of the chaperonin GroEL, and the definition of pathways of chaperone-mediated protein folding.

UI	MeSH Term	Description	Entries
D017510	Protein Folding	Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.	Protein Folding, Globular,Folding, Globular Protein,Folding, Protein,Foldings, Globular Protein,Foldings, Protein,Globular Protein Folding,Globular Protein Foldings,Protein Foldings,Protein Foldings, Globular
D018832	Molecular Chaperones	A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.	Chaperones, Molecular,Chaperone, Molecular,Molecular Chaperone
D018833	Chaperonins	A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences.	Chaperonin,Chaperonin Complex,Chaperonin Complexes,Chaperonin Family,Chaperonin Protein Complex,Complex, Chaperonin
D018840	HSP70 Heat-Shock Proteins	A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.	Heat-Shock Proteins 70,Heat Shock 70 kDa Protein,Heat-Shock Protein 70,HSP70 Heat Shock Proteins,Heat Shock Protein 70,Heat Shock Proteins 70,Heat-Shock Proteins, HSP70