BAIT

HSP90AA1

EL52, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, Hsp89, Hsp90, LAP-2, LAP2
heat shock protein 90kDa alpha (cytosolic), class A member 1
Homo sapiens
PREY

FKBP1A

FKBP-12, FKBP-1A, FKBP1, FKBP12, PKC12, PKCI2, PPIASE, RP11-314N13.2
FK506 binding protein 1A, 12kDa
GO Process (26)
GO Function (11)
GO Component (7)
Homo sapiens

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex.

Oroz J, Chang BJ, Wysoczanski P, Lee CT, Perez-Lara A, Chakraborty P, Hofele RV, Baker JD, Blair LJ, Biernat J, Urlaub H, Mandelkow E, Dickey CA, Zweckstetter M

The molecular chaperone Hsp90 is critical for the maintenance of cellular homeostasis and represents a promising drug target. Despite increasing knowledge on the structure of Hsp90, the molecular basis of substrate recognition and pro-folding by Hsp90/co-chaperone complexes remains unknown. Here, we report the solution structures of human full-length Hsp90 in complex with the PPIase FKBP51, as well as the 280?kDa ... [more]

Nat Commun Dec. 31, 2017; 9(1);4532 [Pubmed: 30382094]

Throughput

  • Low Throughput

Curated By

  • BioGRID