Interconversion between two unrelated protein folds in the lymphotactin native state

By Robbyn L. Tuinstra, F. Peterson, Snježana Kutleša, E. S. Elgin, M. Kron, B. Volkman. 2008

303 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Radiology, Nuclear Medicine and Imaging

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In Immunology

Dorothee Kern

In Molecular Biology

Citations in the corpus

Predicting multiple conformations via sequence clustering and AlphaFold2 (2023, neutral): “Lymphotactin is a human cytokine that adopts a cytokine-like fold but was found to adopt an all-β-sheet dimer as determined using NMR at a higher temperature and in the absence of salt 25 .”
Extant fold-switching proteins are widespread (2018, background): “9% in the PDB), has fostered the discovery of fold switchers by revealing significant chemical shift changes under different conditions (26).”
AlphaFold2 fails to predict protein fold switching (2022, background): “10 Thus, the sequences of fold-switching protein regions encode more than one ordered state.”
Prediction of multiple conformational states by combining sequence clustering with AlphaFold2 (2022, background): “Lymphotactin is a human cytokine that adopts a cytokine-like fold but was found to adopt an all-β -sheet dimer via NMR at higher temperature and in the absence of salt 12 .”
International Union of Basic and Clinical Pharmacology. LXXXIX. Update on the Extended Family of Chemokine Receptors and Introducing a New Nomenclature for Atypical Chemokine Receptors (2014, unknown): “…XCL1 adopts two distinct structures in equilibrium in physiologic solution conditions: one has the canonical chemokine fold and functions as an XCR1 agonist but fails to bind heparin, whereas the second structure binds heparin with high affinity but fails to activate XCR1 (Tuinstra et al., 2008).”
An α-helix to β-barrel domain switch transforms the transcription factor RfaH into a translationfactor (2012, unknown): “Lymphotactin (Ltn) exists in two active conformations under physiological conditions—as amonomer with a chemokine fold and as a dimer with a b sandwich fold—and the interconversion is induced by reorganization of an N-terminal loop to form a b strand interaction while the C-terminal a helix becomes ”
Protein Metamorphosis: The Two-State Behavior of Mad2 (2008, background): “First, the two conformers of Ltn interconvert much more rapidly than the two conformers of Mad2 do (Tuinstra et al., 2008).”
Mutational tipping points for switching protein folds and functions (2012, background): “However, there are a small but growing number of other naturally occurring examples such as lymphotactin (Tuinstra et al., 2008), Mad2 (Luo and Yu, 2008; Mapelli and Musacchio, 2007), and CLIC1 (Littler et al.”
A minimal sequence code for switching protein structure and function (2009, background): “Another recent example is the chemokine lymphotactin, which has 2 populated conformational states under physiologic conditions: the canonical chemokine fold (3-stranded -sheet and C-terminal -helix) in equilibrium with an all -sheet dimer (27).”