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Protein Science, Vol 7, Issue 12 2602-2612, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Localization of basic residues required for receptor binding to the single {alpha}-helix of the receptor binding domain of human {alpha}(2)-macroglobulin

W. HUANG, K. DOLMER, X. LIAO and PGW. GETTINS
Department of Biochemistry and Molecular Biology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60612-4316

To better understand the structural basis for the binding of proteinase-transformed human {alpha}(2)-macroglobulin ({alpha}(2)M) to its receptor, we have used three-dimensional multinuclear NMR spectroscopy to determine the secondary structure of the receptor binding domain (RBD) of human {alpha}(2)M. Assignment of the backbone NMR resonances of RBD was made using (13)C/(15)N and (15)N-enriched RBD expressed in Escherichia coli. The secondary structure of RBD was determined using (1)H and (13)C chemical shift indices and inter- and intrachain nuclear Overhauser enhancements. The secondary structure consists of eight strands in {beta}-conformation and one {alpha}-helix, which together comprise 44% of the protein. The {beta}-strands form three regions of antiparallel {beta}-sheet. The two lysines previously identified as being critical for receptor binding are located in (Lys1374), and immediately adjacent to (Lys1370) the {alpha}-helix, which also contains an (Arg1378). Secondary structure predictions of other {alpha}-macroglobulins show the conservation of this {alpha}-helix and suggest an important role for this helix and for basic residues within it for receptor binding.
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