The energetic landscape of CH–π interactions in protein–carbohydrate binding

Journal Article · 21 January 2025 · Chemical Science

DOI: https://doi.org/10.1039/D4SC06246A · OSTI ID:2504610

Keys, Allison M.  ^[1]; Kastner, David W.  ^[2]; Kiessling, Laura L.  ^[3]; Kulik, Heather J.  ^[4]

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1. Computational and Systems Biology Program, Massachusetts Institute of Technology, Cambridge, MA 02139, USA, Department of Chemical Engineering, MIT, Cambridge, MA 02139, USA, Department of Chemistry, MIT, Cambridge, MA, 02139, USA
2. Department of Chemical Engineering, MIT, Cambridge, MA 02139, USA, Department of Chemistry, MIT, Cambridge, MA, 02139, USA, Department of Biological Engineering, MIT, Cambridge, MA, 02139, USA
3. Department of Chemistry, MIT, Cambridge, MA, 02139, USA, The Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA, Koch Institute for Integrative Cancer Research, MIT, Cambridge, MA 02142, USA
4. Department of Chemical Engineering, MIT, Cambridge, MA 02139, USA, Department of Chemistry, MIT, Cambridge, MA, 02139, USA, The Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA

Over hundreds of PDB structures of protein–sugar complexes, our work demonstrates the prevalence of CH–π stacking interactions, and energetic analysis shows that numerous orientations allow for highly favorable interaction strengths.

• Sponsoring Organization: USDOE
• OSTI ID: 2504610
• Journal Information: Chemical Science, Journal Name: Chemical Science Journal Issue: 4 Vol. 16; ISSN 2041-6520; ISSN CSHCBM
• Publisher: Royal Society of Chemistry (RSC)Copyright Statement
• Country of Publication: United Kingdom
• Language: English