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... > Amino Acids, Peptides, and Proteins > Proteins > Molecular Chaperones > Heat-Shock Proteins > Chaperonins > Group I Chaperonins > Chaperonin 60
... > Enzymes and Coenzymes > Enzymes > Hydrolases > Acid Anhydride Hydrolases > Adenosine Triphosphatases > Chaperonins > Group I Chaperonins > Chaperonin 60

Preferred term

Chaperonin 60  

Type

  • Topical Descriptor

Broader concept

Entry terms

  • Heat Shock Protein 60
  • Heat-Shock Protein 60
  • Heat Shock Proteins 60
  • Heat-Shock Proteins 60
  • hsp60 Family
  • hsp60 Protein

Note

  • coordinate with MITOCHONDRIAL PROTEINS or BACTERIAL PROTEINS if pertinent

Scope note

  • A group I chaperonin protein that forms the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.

History note

  • 1995(1989)

In other languages

URI

http://www.yso.fi/onto/mesh/D018834

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