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Concept information

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

Preferred term

Chaperonin 60  

Type

  • mesh:Descriptor

Definition

  • 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. A chaperonin 60 heat-shock protein isolated from bacteria.

Broader concept

Entry terms

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

Allowable Qualifier(s)

In other languages

  • Chaperonine-60

    French

  • Cpn60
  • Famille des hsp-60
  • Famille hsp60
  • Protéine de choc thermique hsp60
  • Protéine de choc thermique-60
  • Protéine de stress hsp60
  • Protéine de stress-60
  • Protéine hsp60

URI

http://data.loterre.fr/ark:/67375/JVR-XMLVJQ27-V

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RDF/XML TURTLE JSON-LD Created 5/31/94, last modified 1/15/16