Structural highlights
Function
HPBP1_HUMAN Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.[1] [2] [3] [4]
References
- ↑ Raynes DA, Guerriero V Jr. Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein. J Biol Chem. 1998 Dec 4;273(49):32883-8. PMID:9830037
- ↑ Raynes DA, Guerriero V. Isolation and characterization of isoforms of HspBP1, inhibitors of Hsp70. Biochim Biophys Acta. 2000 Jan 31;1490(1-2):203-7. PMID:10786638
- ↑ McLellan CA, Raynes DA, Guerriero V. HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain. J Biol Chem. 2003 May 23;278(21):19017-22. Epub 2003 Mar 21. PMID:12651857 doi:https://dx.doi.org/10.1074/jbc.M301109200
- ↑ Alberti S, Bohse K, Arndt V, Schmitz A, Hohfeld J. The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Mol Biol Cell. 2004 Sep;15(9):4003-10. Epub 2004 Jun 23. PMID:15215316 doi:https://dx.doi.org/10.1091/mbc.E04-04-0293
