Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes

Science

Volumn 350, Issue 6257, 2015, Pages

  Rostislavleva, Ksenia ^a   Soler, Nicolas ^a   Ohashi, Yohei ^a   Zhang, Lufei ^a   Pardon, Els ^b,c   Burke, John E ^a,e   Masson, Glenn R ^a   Johnson, Chris ^a   Steyaert, Jan ^b,c   Ktistakis, Nicholas T ^d   Williams, Roger L ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^c VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^d BABRAHAM INSTITUTE   (United Kingdom)

^e UNIVERSITY OF VICTORIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BECLIN 1; HETERODIMER; LIPOSOME; NANOBODY; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN SERINE THREONINE KINASE VPS15; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); RNA; SUCCINATE DEHYDROGENASE (UBIQUINONE);

CRYSTAL STRUCTURE; MASS SPECTROMETRY; MEMBRANE; PROTEIN;

ANTIBODY PRODUCTION; ARTICLE; CELL GROWTH; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CROSS LINKING; CRYSTAL STRUCTURE; CRYSTALLIZATION; DEUTERIUM HYDROGEN EXCHANGE; ENZYME LINKED IMMUNOSORBENT ASSAY; ENZYME STRUCTURE; FUNGAL CELL CULTURE; GEL FILTRATION; MASS SPECTROMETRY; MEMBRANE BINDING; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN TARGETING; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA PURIFICATION; ULTRA PERFORMANCE LIQUID CHROMATOGRAPHY; CELL MEMBRANE; CHEMISTRY; ENDOSOME; ENZYMOLOGY; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE; ULTRASTRUCTURE; X RAY CRYSTALLOGRAPHY;

CELL MEMBRANE; CLASS III PHOSPHATIDYLINOSITOL 3-KINASES; CRYSTALLOGRAPHY, X-RAY; ENDOSOMES; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; VACUOLAR SORTING PROTEIN VPS15;

EID: 84943521176     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aac7365     Document Type: Article

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