Localization of basic residues required for receptor binding to the single α‐helix of the receptor binding domain of human α2‐macroglobulin
Year: 1998
Type: article
Abstract: To better understand the structural basis for the binding of proteinase-transformed human alpha2-macroglobulin (alpha2M) to its receptor, we have used three-dimensional multinuclear NMR spectroscopy to determine the secondary structure of the receptor binding domain (RBD) of human alpha2M. Assignment of the backbone NMR resonances of RBD was made using 13C/15-N and 15N-enriched RBD expressed in Escherichia coli. The secondary structure of RBD was determined using 1H and 13C 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.
Source: Protein Science
Institution: University of Illinois Chicago
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
Awards: G1150701164, G1651520518, WIDE-BORE 9.4 TESLA NMR SPECTROMETER FOR UW-MADISON, LRP structure and function, G3822938100, National Biological NMR Facility at Madison, Development of 750 MHz Spectroscopy at the National Magnetic Resonance Facility at Madison., National Biomedical NMR Resource at Madison
OpenAlex ID: W2026365622