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  The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains

Brockmann, C., Leitner, D., Labudde, D., Diehl, A., Sievert, V., Buessow, K., et al. (2004). The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains. FEBS Letters, 558(1-3), 101-106. doi:10.1016/S0014-5793(03)01490-X.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-88F4-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-88F5-7
Genre: Journal Article
Alternative Title : FEBS Lett

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 Creators:
Brockmann, Christoph, Author
Leitner, Dietmar, Author
Labudde, Dirk, Author
Diehl, Annette, Author
Sievert, Volker1, Author              
Buessow, Konrad1, Author              
Kühne, Ronald, Author
Oschkinat, Hartmut, Author
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              

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Free keywords: Silencer of death domains; Bcl-associated athanogene 4; Heat shock protein 70; Nuclear magnetic resonance structure; Homology model
 Abstract: The solution structure of an N-terminally extended construct of the SODD BAG domain was determined by nuclear magnetic resonance spectroscopy. A homology model of the SODD-BAG/HSP70 complex reveals additional possible interactions that are specific for the SODD subfamily of BAG domains while the overall geometry of the complex remains the same. Relaxation rate measurements show that amino acids N358–S375 of SODD which were previously assigned to its BAG domain are not structured in our construct. The SODD BAG domain is thus indeed smaller than the homologous domain in Bag1 defining a new subfamily of BAG domains.

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Language(s): eng - English
 Dates: 2004-01-30
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 173715
ISI: 000188817900020
DOI: 10.1016/S0014-5793(03)01490-X
 Degree: -

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Title: FEBS Letters
  Alternative Title : FEBS Lett
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 558 (1-3) Sequence Number: - Start / End Page: 101 - 106 Identifier: ISSN: 0014-5793