Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 37, Issue 4, Pages 321-328Publisher
SPRINGER
DOI: 10.1007/s10858-006-9129-3
Keywords
low density lipoprotein receptor; LDLR gene family; cysteine-rich repeat; ligand-binding domain; calcium cage
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Megalin, an approx. 600 kDa transmembrane glycoprotein that acts as multi-ligand transporter, is a member of the low density lipoprotein receptor gene family. Several cysteine-rich repeats, each consisting of about 40 residues, are responsible for the multispecific binding of ligands. The solution structure of the twelfth cysteine-rich ligand-binding repeat with class A motif found in megalin features two short beta-strands and two helical turns, yielding the typical fold with a I-III, II-V and IV-VI disulfide bridge connectivity pattern and a calcium coordination site at the C-terminal end. The resulting differences in electrostatic surface potential compared to other ligand-binding modules of this gene family, however, may be responsible for the functional divergence.
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