A Single Interfacial Point Mutation Rescues Solution Structure Determination of the Complex of HMG-D with a DNA Bulge

Broadening of signals from atoms at interfaces can often be a limiting factor in applying solution NMR to the structure determination of complexes. Common contributors to such problems include exchange between free and bound states and the increased molecular weight of complexes relative to the free...

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Published inChembiochem : a European journal of chemical biology p. e202400395
Main Authors Hill, Guy, Yang, Ji-Chun, Easton, Laura, Cerdan, Rachel, McLaughlin, Stephen, Stott, Katherine, Travers, Andrew, Neuhaus, David
Format Journal Article
LanguageEnglish
Published Germany 15.08.2024
Subjects
protein-DNA complex
DNA recognition
HMG-box protein
NMR linewidth
NMR spectroscopy
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Summary:Broadening of signals from atoms at interfaces can often be a limiting factor in applying solution NMR to the structure determination of complexes. Common contributors to such problems include exchange between free and bound states and the increased molecular weight of complexes relative to the free components, but another cause that can be more difficult to deal with occurs when conformational dynamics within the interface takes place at an intermediate rate on the chemical shift timescale. In this work we show how a carefully chosen mutation in the protein HMG-D rescued such a situation, making possible high-resolution structure determination of its complex with a dA2 bulge DNA ligand designed to mimic a natural DNA bend, and thereby revealing a new spatial organization of the complex.
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ISSN:1439-4227
1439-7633
1439-7633
DOI:10.1002/cbic.202400395