High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex

Structure

Volumn 21, Issue 10, 2013, Pages 1834-1847

  Back, Régis ^a,e   Dominguez, Cyril ^b,f   Rothé, Benjamin ^a,g   Bobo, Claude ^a   Beaufils, Chrystel ^c   Moréra, Solange ^d   Meyer, Philippe ^d,h   Charpentier, Bruno ^a   Branlant, Christiane ^a   Allain, Frédéric H T ^b   Manival, Xavier ^a  

^a Biopôle de l Université de Lorraine   (France)

^b ETH ZURICH   (Switzerland)

^c LAB DE CHIM PHYS MACROMOLECULAIRE   (France)

^d LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

^e LABORATOIRE DE BIOCHIMIE   (France)

^f UNIVERSITY OF LEICESTER   (United Kingdom)

^g EPFL   (Switzerland)

^h Institut de Biologie Physico Chimique   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CARBOXYLIC ACID; HEAT SHOCK PROTEIN 90; LYSINE; MULTIPROTEIN COMPLEX; PIH1 PROTEIN; R2TP COMPLEX; RNA POLYMERASE; RVB1 PROTEIN; RVB2 PROTEIN; TAH1 PROTEIN; TAH1 TETHERS HSP90 PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

ADDITION REACTION; ARTICLE; CAPPING PHENOMENON; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HIGH RESOLUTION STRUCTURAL ANALYSIS; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN UNFOLDING; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SOLVATION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; HSP90 HEAT-SHOCK PROTEINS; HYDROGEN BONDING; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEAR PROTEINS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 84885431747     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.07.024     Document Type: Article

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