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A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

Nature Structural Biology volume 4, pages 477–482 (1997)Cite this article

Abstract

Hsp90 is a highly specific chaperone for many signal transduction proteins, including steroid hormone receptors and a broad range of protein kinases. The crystal structure of the N-terminal domain of the yeast Hsp90 reveals a dimeric structure based on a highly twisted sixteen stranded β-sheet, whose topology suggests a possible 3D-domain-swapped structure for the intact Hsp90 dimer. The opposing faces of the β-sheets in the dimer define a potential peptide-binding cleft, suggesting that the N-domain may serve as a molecular ‘clamp’ in the binding of ligand proteins to Hsp90.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University College London, Gower Street, London, WC1E 6BT, UK

    Chrisostomos Prodromou & Peter W. Piper

  2. Joint UCL/LICR Crystallography Laboratory, University College London, Gower Street, London, WC1E 6BT, UK

    S. Mark Roe & Laurence H. Pearl

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  1. Chrisostomos Prodromou
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  4. Laurence H. Pearl
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Prodromou, C., Roe, S., Piper, P. et al. A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nat Struct Mol Biol 4, 477–482 (1997). https://doi.org/10.1038/nsb0697-477

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