The PTEN tumor suppressor forms homodimers in solution

Structure

Volumn 23, Issue 10, 2015, Pages 1952-1957

  Heinrich, Frank ^a,c   Chakravarthy, Srinivas ^d,e   Nanda, Hirsh ^a,c   Papa, Antonella ^f,g   Pandolfi, Pier Paolo ^g   Ross, Alonzo H ^h   Harishchandra, Rakesh K ⁱ   Gericke, Arne ⁱ   Lösche, Mathias ^a,b,c  

^a CARNEGIE MELLON UNIVERSITY   (United States)

^b CARNEGIE MELLON UNIVERSITY   (United States)

^c NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY   (United States)

^d ARGONNE NATIONAL LABORATORY   (United States)

^e Illinois Institute of Technology   (United States)

^f MONASH UNIVERSITY   (Australia)

^g HARVARD MEDICAL SCHOOL   (United States)

^h UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

ⁱ Worcester Polytechnic Institute   (United States)

Author keywords

dimer structure; PI3K Akt pathway; protein docking; PTEN phosphatase; SAXS

Indexed keywords

HOMODIMER; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN; SAXS PROTEIN; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG; POLYPHOSPHOINOSITIDE; PROTEIN BINDING; PTEN PROTEIN, HUMAN; RECOMBINANT PROTEIN;

ARTICLE; CANCER INHIBITION; CHEMICAL STRUCTURE; IN VITRO STUDY; MOLECULAR DOCKING; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; BINDING SITE; CELL LINE; CELL MEMBRANE; CHEMISTRY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; HUMAN; METABOLISM; PHOSPHORYLATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; SMALL ANGLE SCATTERING; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

BINDING SITES; CELL LINE; CELL MEMBRANE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; GENE EXPRESSION; HUMANS; MOLECULAR DOCKING SIMULATION; PHOSPHATIDYLINOSITOL PHOSPHATES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PTEN PHOSPHOHYDROLASE; RECOMBINANT PROTEINS; SCATTERING, SMALL ANGLE; X-RAY DIFFRACTION;

EID: 84943581681     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2015.07.012     Document Type: Article

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