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Titolo:
Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein
Autore:
Briknarova, K; Takayama, S; Brive, L; Havert, ML; Knee, DA; Velasco, J; Homma, S; Cabezas, E; Stuart, J; Hoyt, DW; Satterthwait, AC; Llinas, M; Reed, JC; Ely, KR;
Indirizzi:
Burnham Inst, La Jolla, CA 92037 USA Burnham Inst La Jolla CA USA 92037Burnham Inst, La Jolla, CA 92037 USA Battelle Mem Inst, Pacific NW Natl Lab, EMSL, Richland, WA 99352 USA Battelle Mem Inst Richland WA USA 99352 Lab, EMSL, Richland, WA 99352 USA Carnegie Mellon Univ, Dept Chem, Pittsburgh, PA 15213 USA Carnegie Mellon Univ Pittsburgh PA USA 15213 em, Pittsburgh, PA 15213 USA
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 4, volume: 8, anno: 2001,
pagine: 349 - 352
SICI:
1072-8368(200104)8:4<349:SAOBCA>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
HSP70 CHAPERONE ACTIVITY; 3-DIMENSIONAL STRUCTURE; GLUCOCORTICOID RECEPTOR; BCL-2-BINDING PROTEIN; NEGATIVE REGULATOR; COGNATE PROTEIN; ATPASE FRAGMENT; DOWN-REGULATION; CHEMICAL-SHIFT; CELL-DEATH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Ely, KR Burnham Inst, La Jolla, CA 92037 USA Burnham Inst La Jolla CA USA92037 m Inst, La Jolla, CA 92037 USA
Citazione:
K. Briknarova et al., "Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein", NAT ST BIOL, 8(4), 2001, pp. 349-352

Abstract

BAG-family proteins share a conserved protein interaction region, called the 'BAG domain' which binds and regulates Hsp70/Hsc70 molecular chaperones. This family of cochaperones functionally regulates signal transducing proteins and transcription factors important for cell stress responses, apoptosis, proliferation, cell migration and hormone action. Aberrant overexpression of the founding member of this family, BAG1, occurs in human cancers. Inthis study, a structure-based approach was used to identify interacting residues in a BAG1-Hsc70 complex. An Hsc70-binding fragment of BAG1 was shownby multidimensional NMR methods to consist of an antiparallel three-helix bundle. NMR chemical shift experiments marked surface residues on the second (alpha2) and third (alpha3) helices in the BAG domain that are involved in chaperone binding. Structural predictions were confirmed by site-directedmutagenesis of these residues, resulting in loss of binding of BAG1 to Hsc70 in vitro and in cells. Molecular docking of BAG1 to Hsc70 and mutagenesis of Hsc70 marked the molecular surface of the ATPase domain necessary for interaction with BAG1. The results provide a structural basis for understanding the mechanism by which BAG proteins link molecular chaperones and cellsignaling pathways.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 03:15:57