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Crystal structure of chaperone protein PapD reveals an immunoglobulin fold

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Crystal structure of chaperone protein PapD reveals an immunoglobulin fold (English)

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A Holmgren

1

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C I Bränden

series ordinal

2

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language of work or name

English

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publication date

16 November 1989

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published in

Nature

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volume

342

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issue

6247

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page(s)

248-51

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The PapG adhesin of uropathogenic Escherichia coli contains separate regions for receptor binding and for the incorporation into the pilus

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Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution

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A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene

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(Q27690139)

Crystal structure of chaperone protein PapD reveals an immunoglobulin fold

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