ArticleBiochemistry2012
Cation-π interactions in lipocalins: structural and functional implications.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Detection of weak non-covalent cation-π interactions in NGAL by single-molecule force spectroscopy.Nano research · 2022Article
- Tear Lipocalin and Lipocalin-Interacting Membrane Receptor.Frontiers in physiology · 2021Article
- Contribution of cation-π interactions to the stability of Sm/LSm oligomeric assemblies.Protoplasma · 2015Article
- Targeting a cluster of arginine residues of neuraminidase to avoid oseltamivir resistance in influenza A (H1N1): a theoretical study.Journal of molecular modeling · 2015Article
- Exploring protein solution structure: Second moments of fluorescent spectra report heterogeneity of tryptophan rotamers.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2015Article
- Crystal structures of three representatives of a new Pfam family PF14869 (DUF4488) suggest they function in sugar binding/uptake.Protein science : a publication of the Protein Society · 2014Article
- Probing tertiary structure of proteins using single Trp mutations with circular dichroism at low temperature.The journal of physical chemistry. B · 2014Article
- Article
- Tryptophan rotamer distribution revealed for the α-helix in tear lipocalin by site-directed tryptophan fluorescence.The journal of physical chemistry. B · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The cation-π interaction impacts protein folding, structural stability, specificity, and molecular recognition. Cation-π interactions have been overlooked in the lipocalin family. To fill this gap, these interactions were analyzed in the 113 crystal and solution structures from the lipocalin family. The cation-π interactions link previously identified structurally conserved regions and reveal new motifs, which are beyond the reach of a sequence alignment algorithm. Functional and structural significance of the interactions were tested experimentally in human tear lipocalin (TL). TL, a prominent and promiscuous lipocalin, has a key role in lipid binding at the ocular surface. Ligand binding modulation through the loop AB at the "open" end of the barrel has been erroneously attributed solely to electrostatic interactions. Data revealed that the interloop cation-π interaction in the pair Phe28-Lys108 contributes significantly to stabilize the holo-conformation of the loop AB. Numerous energetically significant and conserved cation-π interactions were uncovered in TL and throughout the lipocalin family. Cation-π interactions, such as the highly conserved Trp17-Arg118 pair in TL, were educed in low temperature experiments of mutants with Trp to Tyr substitutions.
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Registered trials
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