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TitleStructural basis for client recognition and activity of Hsp40 chaperones.
Journal, issue, pagesScience, Vol. 365, Page 1313-1319, Year 2019
Publish dateJul 8, 2019 (structure data deposition date)
AuthorsJiang, Y. / Rossi, P. / Kalodimos, C.G.
External linksScience / PubMed:31604242
MethodsNMR (solution)
Structure data

PDB-6ppt:
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Method: SOLUTION NMR

PDB-6pq2:
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Method: SOLUTION NMR

PDB-6pqe:
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Method: SOLUTION NMR

PDB-6pqm:
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Method: SOLUTION NMR

PDB-6pri:
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Method: SOLUTION NMR

PDB-6prj:
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Method: SOLUTION NMR

PDB-6prp:
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Method: SOLUTION NMR

PDB-6prq:
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Method: SOLUTION NMR

PDB-6psi:
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Method: SOLUTION NMR

Source
  • escherichia coli (strain k12) (bacteria)
  • thermus thermophilus (strain hb8 / atcc 27634 / dsm 579) (bacteria)
  • thermus thermophilus (bacteria)
  • escherichia coli (E. coli)
KeywordsCHAPERONE / Client Recognition / CHAPERONE/HYDROLASE / CHAPERONE-HYDROLASE complex / HYDROLASE

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