Chaperoninový protein skupiny I, který tvoří soudkovitou strukturu chaperoninového komplexu. Jedná se o oligomerní protein s charakteristickou strukturou čtrnácti podjednotek uspořádaných do dvou prstenců po sedmi podjednotkách. Protein byl původně studován u bakterií, kde je běžně označován jako protein GroEL.

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.

Anotace

coordinate with MITOCHONDRIAL PROTEINS or BACTERIAL PROTEINS if pertinent

DUI

D018834 MeSH Prohlížeč

CUI

M0028189

Předchozí užití

Heat-Shock Proteins (1989-1994); Bacterial Proteins (1989-1994)

Historická pozn.

1995(1989)

Veřejná pozn.

1995; CHAPERONIN 60 was indexed under BACTERIAL PROTEINS & HEAT-SHOCK PROTEINS 1989-1994; HEAT-SHOCK PROTEIN 60 was indexed under HEAT-SHOCK PROTEINS 1993-1994; HSP60 PROTEIN was indexed under HEAT-SHOCK PROTEINS 1989-1994; for GROEL PROTEIN see GROEL PROTEIN 1995-2009