NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6
Low-density lipoprotein receptor (LDLR) family controls diverse developmental and physiological pathways, including an endocytic cargo function and signaling capacities (Herz and Bock 2002). LDLR family members belong to type I transmembrane proteins that contain repeating modules, including the cysteine-rich repeats (LDL-A), making up the ligand-binding domains, a BP domain formed by six YWTD repeats (β-propeller) and an epidermal growth factor (EGF) repeat. The number and arrangement of these modules vary among family members. LRP5/6, a co-receptor for binding to Wnts in the Wnt signaling pathway, start with a BP domain, which repeats four times, followed by three LDL-A repeats. The extracellular side is anchored on the plasma membrane by a single transmembrane segment, followed by a cytoplasmic tail containing NPXY signals for endocytosis and interaction motifs for a variety of cytoplasmic adaptor and scaffolding proteins (Strickland et al. 2002).
KeywordsChemical Shift Change Flexible Loop Culi W32R Mutation Conserve Lysine Residue
This work is supported by NIH RO1 grants (HL074365 and HL076620 to JW). The authors also thank Ms Victoria Murray for critical reading of the manuscript.
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