Table 1.

Chaperone–substrate and chaperone–chaperone interactions

Interaction	KD (μM)	koff (s−1)	kon (M−1s−1)	Reference(s)
Chaperone–substrate interactions
ttHsp40–PhoA (full length)	10	10	1 × 106	68
ttHsp40–PhoA (individual sites)	NA	100	NA	68
SecB–MBP (full)	0.05	0.05	1 × 106	67
SecB–MBP (individual sites)	4–30	NA	NA	67
SecB–PhoA (full)	0.2	0.1	1 × 106	67
SecB–PhoA (individual sites)	8–40	NA	NA	67
TF–PhoA (full)	~2	~1	1 × 105	124
TF–PhoA (individual sites)	2–14	~50	5 × 106–2 × 107	124
TF–MBP	0.5	~0.05	1 × 105	124
GroEL–Aβ40	70	1,400	2 × 107	86
GroEL–Aβ42	300	880	3 × 106	159
GroEL–SH3 (I)	60	200	3.5 × 106	87
GroEL–PolyQ7	1,300	2,650	2.3 × 106	156
Spy–SH3 (native)	~100	1,000	1 × 107	167
Spy–SH3 (I)	3	40	1.3 × 107	167
Spy–Im7 (native)	21	NA	NA	61
Spy–Im7 (unfolded)	0.3	NA	NA	61
Skp–α-synuclein	1.8	0.004	2,560	23
SecB–α-synunclein	0.7	0.003	2,800	23
Hsc70–α-synuclein	1.6	0.005	3,560	23
Hsp70–hTRF1	18	20	~1 × 106	127, 128
Hsp90–p53	2	NA	NA	127, 128
Skp–Omp4	0.022	NA	NA	54
Hsp90–Tau	5	NA	NA	71
Chaperone–chaperone interactions
ttHsp40–Hsp70 tail	11	NA	NA	68
DNAJB6JD–DNAJB6CTD	NA	530	34a	72
DNAKNBD–ClpBCCD	25	NA	NA	121
Hsp27 ACD dimer	0.5	NA	NA	72
Hsp27 IXI motif	125	NA	NA	2
Hsp90–p23	1	NA	NA	6
Bip–Bap	1	NA	NA	119
CHIP–Hsc70b	0.62	NA	NA	10
CHIP–Hsp90b	1	NA	NA	10
Hop–Hsc70b	2.7	NA	NA	10
Hop–Hsp90b	5.5	NA	NA	10
DNAJC7–Hsc70b	3	NA	NA	10
DNAJC7–Hsp90b	6.8	NA	NA	10

^aIn units of s⁻¹.

^bBased on the interaction of full-length cochaperones with Hsp70/90-derived C-terminal peptides.

Abbreviations: ACD, α-crystallin domain; Bap, nucleotide exchange factor; Bip, endoplasmic Hsp70; CHIP, carboxyl terminus of Hsp70 interacting protein; Hop, Hsp70/Hsp90 organizing proteins; MBP, maltose binding protein; NA, not applicable; PhoA, alkaline phosphatase; PolyQ7, Huntingtin N terminus plus 7 glutamines; SH3 (I), folding intermediate of Fyn SH3; TF, Trigger Factor; ttHsp40, Thermus thermophilus class B Hsp40 (dimer).