ArticleMethods in enzymology2009
Chapter 3. Lymphotactin structural dynamics.
Article in Methods in enzymology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 31 citations in OpenAlex.
- Structural heterogeneity of iron-sulfur cluster scaffold protein IscU: Metamorphic or partially folded?Structural dynamics (Melville, N.Y.) · 2026Review
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
- Post-processing enhances protein secondary structure prediction with second order deep learning and embeddings.Computational and structural biotechnology journal · 2025Article
- Chemokine Heteromers and Their Impact on Cellular Function-A Conceptual Framework.International journal of molecular sciences · 2023Review
- Distinguishing features of fold-switching proteins.Protein science : a publication of the Protein Society · 2023Review
- Specific binding-induced modulation of the XCL1 metamorphic equilibrium.Biopolymers · 2021Article
- Bifurcated Hydrogen Bonds and the Fold Switching of Lymphotactin.The journal of physical chemistry. B · 2020Article
- Unveiling the activation dynamics of a fold-switch bacterial glycosyltransferase byThe Journal of biological chemistry · 2020Article
- Switchable Membrane Remodeling and Antifungal Defense by Metamorphic Chemokine XCL1.ACS infectious diseases · 2020Article
- Transcriptional Profiles of Skeletal Muscle Associated With Increasing Severity of White Striping in Commercial Broilers.Frontiers in physiology · 2020Article
- HIV-1 Reverse Transcriptase: A Metamorphic Protein with Three Stable States.Structure (London, England : 1993) · 2019Review
- Engineering Metamorphic Chemokine Lymphotactin/XCL1 into the GAG-Binding, HIV-Inhibitory Dimer Conformation.ACS chemical biology · 2015Article
- Fast-folding proteins under stress.Cellular and molecular life sciences : CMLS · 2015Review
- Allosteric activation of the Par-6 PDZ via a partial unfolding transition.Journal of the American Chemical Society · 2013Article
- Chemokine oligomerization in cell signaling and migration.Progress in molecular biology and translational science · 2013Review
- Electrostatic optimization of the conformational energy landscape in a metamorphic protein.Biochemistry · 2012Article
- Article
- Structural gymnastics of multifunctional metamorphic proteins.Biophysical reviews · 2011Review
- Article
- Dynamic interchanging native states of lymphotactin examined by SNAPP-MS.Journal of the American Society for Mass Spectrometry · 2011Article
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3 authors at 1 institution in 1 country.
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Abstract
Lymphotactin/XCL1, the defining member of the C class of chemokines, undergoes a conformational change that involves the complete restructuring of all stabilizing interactions. Other chemokines are restricted to a single conformation by a pair of conserved disulfide crosslinks, one of which is absent in lymphotactin. This structural interconversion is entirely reversible, and the two-state equilibrium is sensitive to changes in temperature and ionic strength. One species adopts the conserved chemokine fold as a monomer and functions as an agonist for XCR1, the specific G-protein-coupled receptor for lymphotactin. Rearrangement to the other conformation produces a novel four-stranded sheet that dimerizes to form a beta sandwich with high affinity for cell-surface glycosaminoglycans. We developed methods for resolving the two species and investigated the dynamics of human lymphotactin structural interconversion with NMR spectroscopy, heparin affinity chromatography, and time-resolved fluorescence on the wild-type protein and a panel of amino acid-substituted lymphotactin variants. Our results show that the lymphotactin structural rearrangement occurs at a rate of approximately 1/s and that mutation of residues required for glycosaminoglycan binding shifts the conformational equilibrium toward the chemokine-like fold. We speculate that charge repulsion between arginines 23 and 43 destabilizes the chemokine fold and promotes conversion to the novel lymphotactin dimer, whereas binding of chloride or another anion stabilizes the chemokine fold by neutralizing the repulsive effect.
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