Structural and thermodynamic comparison of the catalytic domain of AMSH and AMSH-LP: Nearly identical fold but different stability

Journal of Molecular Biology

Volumn 413, Issue 2, 2011, Pages 416-429

  Davies, Christopher W ^a   Paul, Lake N ^a   Kim, Myung Il ^a   Das, Chittaranjan ^a  

^a PURDUE UNIVERSITY   (United States)

Author keywords

conformational plasticity; endosomal deubiquitinase; JAMM domain deubiquitinase; Lys63 linked polyubiquitin chain specific deubiquitinase; metalloprotease

Indexed keywords

ESCRT PROTEIN; GUANIDINE; PROTEIN AMSH; PROTEIN AMSH LP; PROTEIN JAMM; UBIQUITINATED PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYME STRUCTURE; PRIORITY JOURNAL; THERMODYNAMICS;

EID: 80054717381     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.08.029     Document Type: Article

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