Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the IXI motif and introduction of the substitution, R107g, in the α-crystallin domain

Philosophical Transactions of the Royal Society B: Biological Sciences

Volumn 368, Issue 1617, 2013, Pages 1-11

  Quinlan, Roy A ^a,b   Zhang, Yan ^c   Lansbury, Andrew ^a,b   Williamson, Ian ^a,b   Pohl, Ehmke ^a,b   Sun, Fei ^c  

^a DURHAM UNIVERSITY   (United Kingdom)

^b DBiophysical Sciences Institute   (United Kingdom)

^c INSTITUTE OF BIOPHYSICS   (China)

Author keywords

Chaperone small heat shock proteins; CRYAB B crystallin R120g; Cryo electron microscopy; Desminopathy crystallinopathy; IXI motif; Structure and function

Indexed keywords

CITRIC ACID; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; PROTEIN;

ANIMALIA; METAZOA;

ALPHA CRYSTALLIN; ARCHAEAL PROTEIN; HEAT SHOCK PROTEIN;

ARCHAEON; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; GENE DELETION; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MOLECULAR CLONING; PHYSIOLOGY; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE;

ALPHA-CRYSTALLINS; AMINO ACID MOTIFS; ARCHAEA; ARCHAEAL PROTEINS; CLONING, MOLECULAR; GENE DELETION; GENE EXPRESSION REGULATION, ARCHAEAL; HEAT-SHOCK PROTEINS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY;

EID: 84875417421     PISSN: 09628436     EISSN: 14712970     Source Type: Journal    
DOI: 10.1098/rstb.2012.0327     Document Type: Article

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