Conserved distal loop residues in the HSP104 and CLPB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation

Journal of Biological Chemistry

Volumn 289, Issue 2, 2014, Pages 848-867

  DeSantis, Morgan E ^a,b,d   Sweeny, Elizabeth A ^a,b   Snead, David ^a,e   Leung, Eunice H ^a,f   Go, Michelle S ^a,g   Gupta, Kushol ^a   Wendler, Petra ^c   Shorter, James ^a,b  

^a Stellar Chance Laboratories   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF MUNICH   (Germany)

^d HARVARD MEDICAL SCHOOL   (United States)

^e WEILL CORNELL MEDICAL COLLEGE   (United States)

^f UNIVERSITY OF HONG KONG   (Hong Kong)

^g UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DISORDERED PROTEINS; HANDOVER; LOOP RESIDUES; NUCLEOTIDE-BINDING DOMAIN; PROTEIN DISAGGREGATION;

BIOCHEMISTRY; BIOLOGY;

PROTEINS;

HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 70; HELIX LOOP HELIX PROTEIN; NUCLEOTIDE BINDING DOMAIN 2; NUCLEOTIDE BINDING PROTEIN; PROTEIN CLPB; PROTEIN DNAK; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN HOMEOSTASIS; PROTEIN PURIFICATION;

CLPB; DISAGGREG; DNA; HSP104; HSP70; MOLECULAR CHAPERONE; PROTEIN AGGREGATION; PROTEIN FOLDING; STRESS; STRESS RESPONSE;

AMINO ACID SEQUENCE; BINDING SITES; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; HOT TEMPERATURE; HSP70 HEAT-SHOCK PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE PROTEINS; SCATTERING, SMALL ANGLE; SEQUENCE HOMOLOGY, AMINO ACID; X-RAY DIFFRACTION;

EID: 84891905978     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.520759     Document Type: Article

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