Structure of WDR5 Bound to Mixed Lineage Leukemia Protein-1 Peptide

• Published in: The Journal of biological chemistry Vol. 283; no. 47; pp. 32158 - 32161
• Main Authors: Patel, Anamika, Dharmarajan, Venkatasubramanian, Cosgrove, Michael S.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 21.11.2008; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Motifs; ARGININE; Arginine - chemistry; Calorimetry; CRYSTAL STRUCTURE; Crystallography, X-Ray; Dimerization; DNA Methylation; Histone-Lysine N-Methyltransferase - chemistry; HISTONES; Histones - chemistry; Humans; INTERACTIONS; Intracellular Signaling Peptides and Proteins; LEUKEMIA; LYSINE; MATERIALS SCIENCE; METHYLATION; Molecular Conformation; Myeloid-Lymphoid Leukemia Protein - chemistry; national synchrotron light source; PEPTIDES; Peptides - chemistry; Protein Conformation; THERMODYNAMICS

The mixed lineage leukemia protein-1 (MLL1) catalyzes histone H3 lysine 4 methylation and is regulated by interaction with WDR5 (WD-repeat protein-5), RbBP5 (retinoblastoma-binding protein-5), and the Ash2L (absent, small, homeotic discs-2-like) oncoprotein. In the accompanying investigation, we des...