Tah1 helix-swap dimerization prevents mixed Hsp90 co-chaperone complexes

Acta Crystallographica Section D: Biological Crystallography

Volumn 71, Issue , 2015, Pages 1197-1206

  Morgan, Rhodri M L ^a   Pal, Mohinder ^a   Roe, S Mark ^a   Pearl, Laurence H ^a   Prodromou, Chrisostomos ^a  

^a UNIVERSITY OF SUSSEX   (United Kingdom)

Author keywords

co chaperones; Hsp90; Tah1

Indexed keywords

CHAPERONE; CYCLOPHILIN; CYCLOPHILIN D; HEAT SHOCK PROTEIN 90; MULTIPROTEIN COMPLEX; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN; TAH1 PROTEIN, S CEREVISIAE;

AMINO ACID SEQUENCE; BINDING SITE; CHEMICAL PHENOMENA; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; MOLECULAR MODEL; PROTEIN DOMAIN; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYCLOPHILINS; HSP90 HEAT-SHOCK PROTEINS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84929246842     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004715004551     Document Type: Article

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