The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains
| Autor: | Dietmar Leitner, Volker Sievert, Ronald Kühne, Dirk Labudde, Annette Diehl, Christoph Brockmann, Hartmut Oschkinat, Konrad Büssow |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
BAG domain
Models Molecular Subfamily Magnetic Resonance Spectroscopy Molecular Sequence Data Static Electricity Biophysics Silencer of death domains Computational biology Biochemistry NMR - Nuclear magnetic resonance Protein Structure Secondary Structural Biology Genetics Heat shock protein 70 Humans Computer Simulation HSP70 Heat-Shock Proteins Homology modeling Amino Acid Sequence Molecular Biology Conserved Sequence Homology model Binding Sites Sequence Homology Amino Acid Chemistry Hydrogen Bonding Cell Biology Models Theoretical Electrostatics Solution structure Bcl-associated athanogene 4 Protein Structure Tertiary Solutions Crystallography Relaxation rate Nuclear magnetic resonance structure |
| Zdroj: | FEBS letters. 558(1-3) |
| ISSN: | 0014-5793 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text