ArticleBiophysical chemistry2010
Excited protein states of human tear lipocalin for low- and high-affinity ligand binding revealed by functional AB loop motion.
Article in Biophysical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Tear Lipocalin and Lipocalin-Interacting Membrane Receptor.Frontiers in physiology · 2021Article
- Ligand binding complexes in lipocalins: Underestimation of the stoichiometry parameter (n).Biochimica et biophysica acta. Proteins and proteomics · 2018Article
- Article
- Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Double tryptophan exciton probe to gauge proximal side chains in proteins: augmentation at low temperature.The journal of physical chemistry. B · 2015Article
- Exploring protein solution structure: Second moments of fluorescent spectra report heterogeneity of tryptophan rotamers.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2015Article
- Probing tertiary structure of proteins using single Trp mutations with circular dichroism at low temperature.The journal of physical chemistry. B · 2014Article
- Cation-π interactions in lipocalins: structural and functional implications.Biochemistry · 2012Article
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Authors and funding
3 authors.
Funding
Abstract
Human tear lipocalin (TL), a prominent member of lipocalin family, exhibits functional and structural promiscuity. The plasticity of loop regions modulates entry to the ligand pocket at the "open" end of the eight-stranded beta-barrel. Site-directed multi-distance measurements using fluorescence resonance energy transfer between functional loops register two excited protein states for low- and high-affinity ligand binding. At low pH, the longest loop AB adopts the conformation of the low-affinity excited protein state that matches the crystal structure of holo-TL at pH 8. A "crankshaft" like movement is detected for the loop AB in a low pH transition. At pH 7.3 the holo-protein assumes a high-affinity excited protein state, in which the loop AB is more compact (RMS=3.1A). In the apo-holo transition, the reporter Trp 28 moves about 4.5A that reflects a decrease in distance between Glu27 and Lys108. This interaction fixes the loop AB conformation for the high-affinity mode. No such movement is detected at low pH, where Glu27 is protonated. Data strongly indicate that the protonation state of Glu27 modulates the conformation of the loop AB for high- and low-affinity binding.
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