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Download pdf summary of Hsp70 related work

Download pdf summary of Dynamics-related work

Download pdf summary of other work

 

DnaJ_comparison.jpg

Binding of DnaJ (white) to Hsp70 in solution  and in the crystal (orange)

 

Ahmad A, Bhattacharya A, McDonald RA, Cordes M, Ellington B, Bertelsen EB, Zuiderweg ER.

Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.

Proc Natl Acad Sci U S A., 108; 18966-18971 (2011)

 

DnaK_vs_Xray.jpg

Structures of Hsp70 proteins in solution (yellow and blue) vs crystal strucures (red and green)

 

Bertelsen, E.B., Chang, L., Gestwicki, J.E. and Zuiderweg, E.R.P. “Solution conformation of E.coli Hsp70 complexed with ADP and substrate”.  Proc. Natl. Acad. Sci. 106, 8471-8476 (2009)

 

Revington, M., Zhang, Yip, G.N.B., Kurochkin, A.V. and Zuiderweg, E.R.P.  NMR investigations of allosteric processes in a two-domain Thermus Thermophilus Hsp70 molecular chaperone, J. Mol. Biol. 349, 163-183 (2005)

 

NBD_conformations_XRAY.jpg

TTH_CONFORMATIONs.jpg

ATP/ADP conformational change in Hsp70 in the crystal (left) and in solution (right)

 

Bhattacharya, A., Kurochkin, A.V., Yip, G.N.B., Zhang, Y., Bertelsen, E.B.  and Zuiderweg. E.R.P. Allostery in the Hsp70 chaperones is transduced by subdomain rotations.

J. Mol. Biol. 388, 475-90, 2009

 

final_amber_dock_shifts.jpg

Binding site of the anti-cancer drug MKT-077 (cyan)  to Hsp70

 

Rousaki A, Miyata Y, Jinwal UK, Dickey CA, Gestwicki JE, Zuiderweg ER.

Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones.

J Mol Biol., 411, 614-632. (2011)

 

 

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