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Structural Basis for LMO2-Driven Recruitment of the SCL:E47bHLH Heterodimer to Hematopoietic-Specific Transcriptional Targets

DOI: 10.1016/j.celrep.2013.06.008 DOI Help
PMID: 23831025 PMID Help

Authors: Kamel El Omari (The Wellcome Trust Centre for Human Genetics, University of Oxford) , Sarah j. Hoosdally (Weatherall Institute of Molecular Medicine, University of Oxford) , Kapil Tuladhar (Weatherall Institute of Molecular Medicine, University of Oxford) , Dimple Karia (University of Oxford) , Elisa Hall-ponselé (Weatherall Institute of Molecular Medicine, University of Oxford) , Olga Platonova (University of Oxford) , Paresh Vyas (Weatherall Institute of Molecular Medicine, University of Oxford) , Roger Patient (Weatherall Institute of Molecular Medicine, University of Oxford) , Catherine Porcher (Weatherall Institute of Molecular Medicine, University of Oxford) , Erika Mancini (The Wellcome Trust Centre for Human Genetics, University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Cell Reports , VOL 4 (1) , PAGES 135 - 147

State: Published (Approved)
Published: July 2013

Open Access Open Access

Abstract: Structure of the quaternary complex SCL:E47:LMO2:LDB1 bound to DNA Identification of SCL:E47:LMO2 interface residues critical for in vivo function LMO2 strengthens SCL:E47 dimerization and modulates DNA-binding activities Structural basis for the E47 sequestration model in blood development and leukemia

Journal Keywords: Animals; Binding; Cell; Tumor; DNA; HEK293; Hematopoiesis; Humans; LIM; Mice; Molecular; Molecular; Mutation; Protein; Transcription; Genetic; Zebrafish

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I02-Macromolecular Crystallography , I04-Macromolecular Crystallography

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