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-Structure paper
Title | The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. |
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Journal, issue, pages | Embo J., Vol. 31, Page 1506-1517, Year 2012 |
Publish date | Nov 17, 2011 (structure data deposition date) |
Authors | Schmid, A.B. / Lagleder, S. / Grawert, M.A. / Rohl, A. / Hagn, F. / Wandinger, S.K. / Cox, M.B. / Demmer, O. / Richter, K. / Groll, M. ...Schmid, A.B. / Lagleder, S. / Grawert, M.A. / Rohl, A. / Hagn, F. / Wandinger, S.K. / Cox, M.B. / Demmer, O. / Richter, K. / Groll, M. / Kessler, H. / Buchner, J. |
External links | Embo J. / PubMed:22227520 |
Methods | NMR (solution) / X-ray diffraction |
Resolution | 1.6 - 2.6 Å |
Structure data | PDB-2llv: PDB-2llw: PDB-3upv: PDB-3uq3: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | CHAPERONE / DP domain / Alpha helix / PEPTIDE BINDING PROTEIN / TPR-fold / Adaptor protein for Hsp70 and Hsp90 / C-terminal part of Hsp70 / Hsp90 / peptide binding |