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Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements

Article Abstract:

A combination of electron microscopy and x-ray crystallography are used to describe the structures of full-length HtpG, the Escherichia coli hsp90 ortholog, revealing dramatic nucleotide-dependent structural rearrangements, from an open conformation in the nucleotide-free state that is accessible to client proteins, to a compact ADP-bound state. The results reveal a general mechanism by which nucleotide binding and hydrolysis control the binding and release hsp90 client proteins.

Author: Agard, David A., Shiau, Andrew K., Harris, Seth F., Southworth, Daniel R.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
Escherichia coli, X-ray crystallography, Structure

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A structural superfamily of growth factors containing a cystine knot motif

Article Abstract:

Structural analyses of nerve growth factor, transforming growth factor beta and platelet-derived growth factor revealed how the prototypical members of three supposedly unrelated families adopt similar protomeric folds that contain the cystine knot motif. These growth factors form a new structural superfamily since the cystine knot was found to be unique to them. The evolutionary implications of the structure of these molecules are discussed.

Author: Hendrickson, Wayne A., McDonald, Neil Q.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
Molecular structure, Transforming growth factors, Nerve growth factor, Platelet-derived growth factor

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Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN

Article Abstract:

Cryo-electron microscopy at 25 A resolution was used for the determination of the structure of dengue virus (DENV) in complex with the carbohydrate recognition domain (CRD) of dendritic cell-specific ICAM3 grabbing noninteger (DC-SIGN). One CRD monomer bounded two glycosylation sites at Asn67 of two neighboring glycoproteins in each isothermal asymmetric unit while the third Asn67 residue remained vacant.

Author: Rossmann, Michael G., Hendrickson, Wayne A., Chipman, Paul R., Ying Zhang, Pokidysheva, Elena, Battisti, Anthony J., Bator-Kelly, Carol M., Chuan Xiao, Gregorio, G. Glenn, Kuhn, RIchard J.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
New York, Glycosylation, Dengue viruses, Dengue virus, Flaviviruses

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Subjects list: Research, Usage, Electron microscopy, Analysis
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