Journal
ANALYTICAL CHEMISTRY
Volume 90, Issue 21, Pages 12796-12801Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.8b03263
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Funding
- National Institutes of Health [NIH R01GM113658]
- National Science Foundation (NSF) [DBI 1455654]
- German Research Foundation (DFG)
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Surface-induced dissociation (SID) is a powerful means of deciphering protein complex quaternary structures due to its capability of yielding dissociation products that reflect the native structures of protein complexes in solution. Here we explore the suitability of SID to locate the ligand binding sites in protein complexes. We studied C-reactive protein (CRP) pentamer, which contains a ligand binding site within each subunit, and cholera toxin B (CTB) pentamer, which contains a ligand binding site between each adjacent subunit. SID dissects ligand-bound CRP into subcomplexes with each subunit carrying predominantly one ligand. In contrast, SID of ligand-bound CTB results in the generation of subcomplexes with a ligand distribution reflective of two subunits contributing to each ligand binding site. SID thus has potential application in localizing sites of small ligand binding for multisubunit protein-ligand complexes.
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