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          Institute: MPI für medizinische Forschung     Collection: Abteilung Biomolekulare Mechanismen     Display Documents



ID: 22960.0, MPI für medizinische Forschung / Abteilung Biomolekulare Mechanismen
Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange
Translation of Title:Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange
Authors:Brehmer, Dirk; Rüdiger, Stefan; Gässler, Claudia S.; Klostermeier, Dagmar; Packschies, Lars; Reinstein, Jochen; Mayer, Matthias P.; Bukau, Bernd
Language:English
Date of Publication (YYYY-MM-DD):2001-05
Title of Journal:Nature Structural Biology
Journal Abbrev.:Nat. Struct. Biol.
Volume:8
Issue / Number:5
Start Page:427
End Page:432
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:The Hsp70 chaperone activity in protein folding is regulated by ATP-controlled cycles of substrate binding and release. Nucleotide exchange plays a key role in these cycles by triggering substrate release. Structural searches of Hsp70 homologs revealed three structural elements within the ATPase domain: two salt bridges and an exposed loop. Mutational analysis showed that these elements control the dissociation of nucleotides, the interaction with exchange factors and chaperone activity. Sequence variations in the three elements classify the Hsp70 family members into three subfamilies, DnaK proteins, HscA proteins and Hsc70 proteins. These subfamilies show strong differences in nucleotide dissociation and interaction with the exchange factors GrpE and Bag-1.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/
Identifiers:URI:http://www.nature.com/cgi-taf/DynaPage.taf?file=/n... [Full text]
URI:http://www.nature.com/cgi-taf/DynaPage.taf?file=/n... [Abstract]
URI:http://www.nature.com/cgi-taf/DynaPage.taf?file=/n... [Fulltext PDF]
DOI:10.1038/87588
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