Fig. 4: ADP binds to the Hsp90 dimers in all PINK1-bound complexes. | Nature Communications

Fig. 4: ADP binds to the Hsp90 dimers in all PINK1-bound complexes.

From: Molecular mechanism of PINK1 regulation by the Hsp90 machinery

Fig. 4

a The density map of ADP and the conserved residues that are crucial for nucleotide binding in the Hsp90-Cdc37-PINK1 complex (colored in green). b The density map of ADP and the surrounding conserved residues in the Hsp90-FKBP51-PINK1 complex (colored in brown). c The density map of ADP and the surrounding conserved residues in the Hsp90 -PINK1 complex (colored in dark brown). d The density map of ADP and the surrounding conserved residues observed in the mitochondrial Hsp90 homolog, TRAP1 (PDB: 5TVX) (colored in pink). e The density map of ATP and the surrounding conserved residues observed in the mitochondrial Hsp90 homolog, TRAP1 (PDB: 5TVU) (colored in light green). f The density map of ATP and the surrounding conserved residues observed in the Hsp90-FKBP51-GR (PDB: 8FFW) (colored in cyan blue). g The density map of ATP and the surrounding conserved residues observed in the Hsp90-Cdc37-CDK4 complex (PDB: 5FWK) (colored in blue). The nucleotides in the above structures are colored in purple red. The black dash lines represent hydrogen bonds.

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