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- W2076945013 endingPage "1614" @default.
- W2076945013 startingPage "1606" @default.
- W2076945013 abstract "DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote protein folding, interaction, and translocation, both constitutively and in response to stress, by binding to unfolded polypeptide segments. These proteins have two functional units: a substrate-binding portion binds the polypeptide, and an adenosine triphosphatase portion facilitates substrate exchange. The crystal structure of a peptide complex with the substrate-binding unit of DnaK has now been determined at 2.0 Å resolution. The structure consists of a β-sandwich subdomain followed by α-helical segments. The peptide is bound to DnaK in an extended conformation through a channel defined by loops from the β sandwich. An α-helical domain stabilizes the complex, but does not contact the peptide directly. This domain is rotated in the molecules of a second crystal lattice, which suggests a model of conformation-dependent substrate binding that features a latch mechanism for maintaining long lifetime complexes." @default.
- W2076945013 created "2016-06-24" @default.
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- W2076945013 creator A5062931824 @default.
- W2076945013 creator A5074571668 @default.
- W2076945013 date "1996-06-14" @default.
- W2076945013 modified "2023-10-09" @default.
- W2076945013 title "Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK" @default.
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- W2076945013 doi "https://doi.org/10.1126/science.272.5268.1606" @default.
- W2076945013 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5629921" @default.
- W2076945013 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8658133" @default.
- W2076945013 hasPublicationYear "1996" @default.
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