Selected article for: "co factor and middle domain"
Author: Wang, Yuan; Li, Yan; Ding, Tianbing
Title: Heat shock protein 90ß in the Vero cell membrane binds Japanese encephalitis virus
  • Document date: 2017_6_26
    • ID: 7cpxg1b4_29
    Snippet: No accurate HSP90β structure is available, even though it shares significant protein homology with its isoform HSP90α, which performs conservative functions in cells by forming homodimers. The crystal structures indicate that HSP90α contains 3 functional domains: a highly conserved N-terminal domain (NTD) of approximately 25 kDa, a middle domain (MD) of approximately 40 kDa and a C-terminal domain (CTD) of approximately 12 kDa. The NTD exhibit.....
    Document: No accurate HSP90β structure is available, even though it shares significant protein homology with its isoform HSP90α, which performs conservative functions in cells by forming homodimers. The crystal structures indicate that HSP90α contains 3 functional domains: a highly conserved N-terminal domain (NTD) of approximately 25 kDa, a middle domain (MD) of approximately 40 kDa and a C-terminal domain (CTD) of approximately 12 kDa. The NTD exhibits a common ATP binding pocket that is shared among HSP90 chaperone family members and is recognised by its natural inhibitor, geldanamycin and its analogues (46, 47) , which target the adenosine triphosphatase (ATPase activity) of the NTD region. The MD is involved in client protein binding involving, for example, PKB/Akt1 and eNOS (48, 49) . The CTD features an alternative ATP-binding site that is only accessible when the N-terminal ATP-binding pocket is occupied (50) . The CTD is also involved in protein binding because it includes the tetratricopeptide repeat (TPR) motif recognition site and conserved MEEVD pentapeptide that is responsible for co-factor interactions, including the immunophilins, stress-induced phosphoprotein 1 (Sti1/Hop), cyclophilin-40, PP5 and Tom70 (51) (52) (53) .

    Search related documents:
    Co phrase search for related documents
    • adenosine triphosphatase and ATPase activity adenosine triphosphatase: 1, 2
    • ATP bind and ATPase activity: 1
    • ATP bind and bind pocket: 1
    • ATP bind pocket and bind pocket: 1
    • ATPase activity and crystal structure: 1, 2
    • bind pocket and crystal structure: 1, 2, 3, 4
    • co factor and crystal structure: 1, 2