Title : Conformational changes in the GroEL oligomer during the functional cycle.

Pub. Date : 1997 Feb

PMID : 9087913






2 Functional Relationships(s)
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1 Average side views of the three allosteric states (TT, TR, and RR, which correspond to none, one, or both of the two heptameric rings of the GroEL oligomer occupied by nucleotide, respectively) of GroEL and GroEL-GroES complexes for ADP, ATP, and two nonhydrolyzable analogs (AMP-PNP and ATP gamma S) have been obtained at 20-25 A resolution. adenosine 5'-O-(3-thiotriphosphate) heat shock protein family D (Hsp60) member 1 Homo sapiens
2 Average side views of the three allosteric states (TT, TR, and RR, which correspond to none, one, or both of the two heptameric rings of the GroEL oligomer occupied by nucleotide, respectively) of GroEL and GroEL-GroES complexes for ADP, ATP, and two nonhydrolyzable analogs (AMP-PNP and ATP gamma S) have been obtained at 20-25 A resolution. adenosine 5'-O-(3-thiotriphosphate) heat shock protein family D (Hsp60) member 1 Homo sapiens