Single-particle EM reveals extensive conformational variability of the Ltn1 E3 ligase

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 5, 2013, Pages 1702-1707

  Lyumkis, Dmitry ^a   Doamekpor, Selom K ^b   Bengtson, Mario H ^b   Lee, Joong Won ^a   Toro, Tasha B ^c   Petroski, Matthew D ^c   Lima, Christopher D ^b   Potter, Clinton S ^a   Carragher, Bridget ^a   Joazeiro, Claudio A P ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^c BURNHAM INSTITUTE   (United States)

Author keywords

Conformational heterogeneity; Ltn1 Listerin; Neurodegenerative disease; RING E3 ubiquitin ligase; Translational surveillance

Indexed keywords

LTN1 LIGASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BIOINFORMATICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN STRUCTURE;

CARRIER PROTEINS; CULLIN PROTEINS; HUMANS; IMAGING, THREE-DIMENSIONAL; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; PARTICLE SIZE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES;

EID: 84873130995     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1210041110     Document Type: Article

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