ArticleThe Journal of biological chemistry2002
Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions.
Article in The Journal of biological chemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 79 citations in OpenAlex.
- Article
- The multifaceted role of XCL1 in health and disease.Protein science : a publication of the Protein Society · 2025Review
- Molecular basis for chemokine recognition and activation of XCR1.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Reversible switching between two common protein folds in a designed system using only temperature.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Design and discovery of metamorphic proteins.Current opinion in structural biology · 2022Review
- Design principles of protein switches.Current opinion in structural biology · 2022Review
- Review
- Specific binding-induced modulation of the XCL1 metamorphic equilibrium.Biopolymers · 2021Article
- Metamorphic proteins: the Janus proteins of structural biology.Open biology · 2021Article
- Fragile protein folds: Sequence and environmental factors affecting the equilibrium of two interconverting, stably folded protein conformations.Magnetic resonance (Gottingen, Germany) · 2021Article
- Evolution of fold switching in a metamorphic protein.Science (New York, N.Y.) · 2021Article
- Bifurcated Hydrogen Bonds and the Fold Switching of Lymphotactin.The journal of physical chemistry. B · 2020Article
- Switchable Membrane Remodeling and Antifungal Defense by Metamorphic Chemokine XCL1.ACS infectious diseases · 2020Article
- Structural Features of an Extended C-Terminal Tail Modulate the Function of the Chemokine CCL21.Biochemistry · 2020Article
- Structure-function guided modeling of chemokine-GPCR specificity for the chemokine XCL1 and its receptor XCR1.Science signaling · 2019Article
- The Solution Structure of CCL28 Reveals Structural Lability that Does Not Constrain Antifungal Activity.Journal of molecular biology · 2018Article
- Structure-Function Relationship of XCL1 Used forFrontiers in immunology · 2018Article
- A Requirement for Metamorphic Interconversion in the Antimicrobial Activity of Chemokine XCL1.Biochemistry · 2016Article
- Engineering Metamorphic Chemokine Lymphotactin/XCL1 into the GAG-Binding, HIV-Inhibitory Dimer Conformation.ACS chemical biology · 2015Article
- Structural Determinants for the Selective Anti-HIV-1 Activity of the All-β Alternative Conformer of XCL1.Journal of virology · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
NMR spectra of human lymphotactin (hLtn), obtained under various solution conditions, have revealed that the protein undergoes a major conformational rearrangement dependent on temperature and salt concentration. At high salt (200 mm NaCl) and low temperature (10 degrees C), hLtn adopts a chemokine-like fold, which consists of a three-stranded antiparallel beta-sheet and a C-terminal alpha-helix (Kuloğlu, E. S., McCaslin, D. R., Kitabwalla, M., Pauza, C. D., Markley, J. L., and Volkman, B. F. (2001) Biochemistry 40, 12486-12496). We have used NMR spectroscopy, sedimentation equilibrium, and intrinsic fluorescence to monitor the reversible conformational change undergone by hLtn as a function of temperature and ionic strength. We have used two-, three- and four-dimensional NMR spectroscopy of isotopically enriched protein samples to determine structural properties of the conformational state stabilized at 45 degrees C and 0 mm NaCl. Patterns of NOEs and (1)H(alpha) and (13)C chemical shifts show that hLtn rearranges under these conditions to form a four-stranded, antiparallel beta-sheet with a pattern of hydrogen bonding that is completely different from that of the chemokine fold stabilized at 10 degrees C and 200 mm NaCl. The C-terminal alpha-helix observed at 10 degrees C and 200 mm NaCl, which is conserved in other chemokines, is absent at 45 degrees C and no salt, and the last 38 residues of the protein are completely disordered, as indicated by heteronuclear (15)N-(1)H NOEs. Temperature dependence of the tryptophan fluorescence of hLtn in low and high salt confirmed that the chemokine conformation is stabilized by increased ionic strength. Sedimentation equilibrium analytical ultracentrifugation showed that hLtn at 40 degrees C in the presence of 100 mm NaCl exists mainly as a dimer. Under near physiological conditions of temperature, pH, and ionic strength, both the chemokine-like and non-chemokine-like conformations of hLtn are significantly populated. The functional relevance of this structural interconversion remains to be elucidated.
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