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The Crystal Structure of a GroEL/Peptide Complex

Open access
Chen, Lingling, Sigler, Paul B·1999·Cell

Abstract

The chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilitates protein folding with an ATP-dependent mechanism. Nonnative conformations of diverse protein substrates bind to the apical domains surrounding the opening of the double toroid's central cavity. Using phage display, we have selected peptides with high affinity for the isolated apical domain. We have determined the crystal structures of the complexes formed by the most strongly bound peptide with the isolated apical domain, and with GroEL. The peptide interacts with the groove between paired alpha helices in a manner similar to that of the GroES mobile loop. Our structural analysis, combined with other results, suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into the shielded cis assembly.

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Metadata

Authors
Chen, L., & Sigler, P. B.
Venue
Cell
Publisher
Elsevier BV
Published
1999-12
Volume
99
Issue
7
Pages
757-768
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2039486080
Cited by
241
References
0
FWCI
7.94
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: The Crystal Structure of a GroEL/Peptide Complex. https://app.cochat.ai/papers/10.1016/s0092-8674(00)81673-6
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Chen, L., & Sigler, P. B. (1999). The Crystal Structure of a GroEL/Peptide Complex. Cell. https://doi.org/10.1016/s0092-8674(00)81673-6

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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