Table 3.
Co-chaperone | Structure of the co-chaperone (A) | Structure of the complex with Hsp70 (B) |
---|---|---|
Bag1 | 1HX1a | 1HX1a |
Bag2 | 3D0Tb | 3CQXc |
CHIP | 2C2Ld | 4KBQe |
GrpE | 3A6Mf (from Thermus thermophilus)1DKGg (from E.coli) | 1DKGg |
HOP | 2NC9h | 1ELWi |
Hsp40 | 1XBLj | 5NROk |
HspBP1 | 1XQRl | 1XQSm |
Hsp110 | 2QXLn | 3D2Fo |
Hip | 4J8D, 4J8Ep | 4J8Fq |
aComplex of the BAG domain (residues 151-264) of BAG1M with the NBD domain (residue 5-381) of Hsc70. 116
bBNB domain (residues 107–189) of murine BAG2.
cComplex of BNB domain (residues 107–189) of murine Bag2 with Hsc70 NBD domain (residues 1-381).
dNear full length structure of CHIP (residues 25-304) from mouse. 117
eComplex structure contains the CHIP-TPR domain (residues 21-154) and Hsp70 lid-tail domain (residues 541-646 Δ626-638). 87
fCrystal structure of GrpE from Thermus thermophilus HB8. 118
gComplex of GrpE (residues 1-197) and NBD domain of DnaK (residues 1-388) from E.coli. 119
hTPR2A domain (residues 220-350) of Hop.
iComplex of TPR1 domain (residues 1-118) of Hop with C-terminal Hsc70 peptide(residues 625-732). 50
jJ domain(residues 2-76) of DNAj. 120
kComplex of J domain (residues 3-65) of Hsp40 with DnaK (residues 2–604). 71
lCrystal structure of core domain of human HspBP1. 96
mCrystal structure of the HspBP1 core domain (residues 84-359) complexed with the lobe II of Hsp70 NBD domain (183–371 residues). 96
nYeast homolog Hsp110: Sse1 (residues 2–659). 108
oComplex of Yeast homolog Hsp110: Sse1p (residues 2–659 and Δ503–524) with NBD (residues 1–377) of yeast Hsp70 homolog Ssa1p. 121
pTPR domain (residues 78–247) of Hip. 111
qComplex of TPR domain (residues 78–247) of Hip and the NBD domain (residues 1–382, point mutation D110E) of Hsp70. 111