D
IPR006636

Heat shock chaperonin-binding

InterPro entry
Short nameSTI1_HS-bd
Overlapping
homologous
superfamilies
 

Description

This entry represents a heat shock chaperonin-binding domain found in human Stress-inducible phosphoprotein STI1 and similar sequences found in eukaryotes. STI1 acts as a co-chaperone for HSP90AA1
[2]
. Both N- and C-terminal ends of STI1 are capable of binding heat shock proteins
[1]
. This domain is found both singly and duplicated in different proteins. This domain shows an α-helical structure
[3]
.

References

1.Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases. Lassle M, Blatch GL, Kundra V, Takatori T, Zetter BR. J. Biol. Chem. 272, 1876-84, (1997). View articlePMID: 8999875

2.The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding. Woodford MR, Dunn DM, Blanden AR, Capriotti D, Loiselle D, Prodromou C, Panaretou B, Hughes PF, Smith A, Ackerman W, Haystead TA, Loh SN, Bourboulia D, Schmidt LS, Marston Linehan W, Bratslavsky G, Mollapour M. Nat Commun 7, 12037, (2016). PMID: 27353360

3.Structure of Hsp90-Hsp70-Hop-GR reveals the Hsp90 client-loading mechanism. Wang RY, Noddings CM, Kirschke E, Myasnikov AG, Johnson JL, Agard DA. Nature 601, 460-464, (2022). PMID: 34937942

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