1CKR Chaperone date Apr 22, 1999
title High Resolution Solution Structure Of The Heat Shock Cognate-70 Kd Substrate Binding Domain Obtained By Multidimensional Nmr Techniques
authors R.C.Morshauser, W.Hu, H.Wang, Y.Pang, G.C.Flynn, E.R.P.Zuiderweg
compound source
Molecule: Heat Shock Substrate Binding Domain Of Hsc-70
Chain: A
Fragment: Substrate Binding Domain
Engineered: Yes
 Organism_scientific: Rattus Norvegicus
Organism_common: Rat
Expression_system: Escherichia Coli
Expression_system_strain: Jm109(De3)
methodNMR, 20 Structures
similarity Belongs to the heat shock protein 70 family.[HSP70]
subunit Interacts with pacrg (by similarity).
induction Constitutively synthesized.
subcellular loc. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock (by similarity).
genes Hsc73, Hspa8 (R. norvegicus)
function Chaperone.
Gene
Ontology
ChainFunctionProcessComponent
A
  • nucleotide binding
  • ATP binding
  • unfolded protein binding
  • protein folding
  • response to unfolded protein...
  • nucleus
    • Primary referenceHigh-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70., Morshauser RC, Hu W, Wang H, Pang Y, Flynn GC, Zuiderweg ER, J Mol Biol 1999 Jun 25;289(5):1387-403. PMID:10373374
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (839 Kb) [Save to disk]
  • Biological Unit Coordinates (1ckr.pdb1.gz) 820 Kb
  • CSU: Contacts of Structural Units for 1CKR
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