HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain

Journal of Biological Chemistry

Volumn 278, Issue 21, 2003, Pages 19017-19022

  McLellan, Catherine A ^a   Raynes, Deborah A ^b   Guerriero, Vince ^a,b  

^a University of Arizona   (United States)

^b UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOASSAY; CONFORMATIONS; ENZYME INHIBITION; PROTEINS;

CIRCULAR DICHROISM;

AMINO ACIDS;

ADENOSINE TRIPHOSPHATASE; AMINO ACID; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN BP1; LUCIFERASE; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; CHYMOTRYPSIN; HSPBP1 PROTEIN, HUMAN; PROTEINASE K; RECOMBINANT PROTEIN; TRYPSIN;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENZYME RENATURATION; EXON; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; RETICULOCYTE LYSATE; CHEMISTRY; DRUG ANTAGONISM; DRUG EFFECT; GENE EXPRESSION REGULATION; GENETICS; HUMAN; MASS SPECTROMETRY; METABOLISM; PROTEIN RENATURATION; PROTEIN SECONDARY STRUCTURE; RETICULOCYTE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; CARRIER PROTEINS; CHYMOTRYPSIN; CIRCULAR DICHROISM; ENDOPEPTIDASE K; EXONS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; LUCIFERASES; MASS SPECTROMETRY; MUTAGENESIS, INSERTIONAL; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN RENATURATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; RETICULOCYTES; STRUCTURE-ACTIVITY RELATIONSHIP; TRYPSIN;

EID: 0038482018     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M301109200     Document Type: Article

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