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Structure paper

TitleThe novolactone natural product disrupts the allosteric regulation of hsp70.
Journal, issue, pagesChem. Biol., Vol. 22, Page 87-97, Year 2015
Publish dateNov 4, 2014 (structure data deposition date)
AuthorsHassan, A.Q. / Kirby, C.A. / Zhou, W. / Schuhmann, T. / Kityk, R. / Kipp, D.R. / Baird, J. / Chen, J. / Chen, Y. / Chung, F. ...Hassan, A.Q. / Kirby, C.A. / Zhou, W. / Schuhmann, T. / Kityk, R. / Kipp, D.R. / Baird, J. / Chen, J. / Chen, Y. / Chung, F. / Hoepfner, D. / Movva, N.R. / Pagliarini, R. / Petersen, F. / Quinn, C. / Quinn, D. / Riedl, R. / Schmitt, E.K. / Schitter, A. / Stams, T. / Studer, C. / Fortin, P.D. / Mayer, M.P. / Sadlish, H.
External linksChem. Biol. / PubMed:25544045
MethodsX-ray diffraction
Resolution2.04 - 2.42 Å
Structure data

PDB-4wv5:
HEAT SHOCK PROTEIN 70 SUBSTRATE BINDING DOMAIN
Method: X-RAY DIFFRACTION / Resolution: 2.04 Å

PDB-4wv7:
HEAT SHOCK PROTEIN 70 SUBSTRATE BINDING DOMAIN WITH COVALENTLY LINKED NOVOLACTONE
Method: X-RAY DIFFRACTION / Resolution: 2.42 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-3UM:
(5beta,6alpha,8alpha,14alpha)-13-ethenyl-5,6-dihydroxy-14-methylpodocarp-12-en-15-oic acid

Source
  • homo sapiens (human)
KeywordsCHAPERONE / chaperone/chaperone inhibitor / Allosteric Inhibitor / chaperone-chaperone inhibitor complex

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