ArticleJournal of molecular biology2008
The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 46 citations in OpenAlex.
- Residual flexibility in the topologically constrained multivalent complex between the GKAP scaffold and LC8 hub proteins.The FEBS journal · 2026Article
- Article
- Dynamic interactions of dimeric hub proteins underlie their diverse functions and structures: A comparative analysis of 14-3-3 and LC8.The Journal of biological chemistry · 2025Review
- Article
- Review
- Quantifying cooperative multisite binding in the hub protein LC8 through Bayesian inference.PLoS computational biology · 2023Article
- Crystal structure of human LC8 bound to a peptide from Ebola virus VP35.Journal of microbiology (Seoul, Korea) · 2021Article
- Structural atlas of dynein motors at atomic resolution.Biophysical reviews · 2018Review
- Normal mode analysis as a method to derive protein dynamics information from the Protein Data Bank.Biophysical reviews · 2017Review
- Dynamical persistence of active sites identified in maltose-binding protein.Journal of molecular modeling · 2017Article
- Genetic diversity and selection of three nuclear genes in Schistosoma japonicum populations.Parasites & vectors · 2017Article
- Fasciola hepatica calcium-binding protein FhCaBP2: structure of the dynein light chain-like domain.Parasitology research · 2016Article
- The Anchored Flexibility Model in LC8 Motif Recognition: Insights from the Chica Complex.Biochemistry · 2016Article
- Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds.FEBS letters · 2015Review
- The mechanism of dynein light chain LC8-mediated oligomerization of the Ana2 centriole duplication factor.The Journal of biological chemistry · 2014Article
- NMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein.Computational and structural biotechnology journal · 2014Review
- Structural features of LC8-induced self-association of swallow.Biochemistry · 2013Article
- The yeast dynein Dyn2-Pac11 complex is a dynein dimerization/processivity factor: structural and single-molecule characterization.Molecular biology of the cell · 2013Article
- Structural analysis of the regulation of the DYNLL/LC8 binding to Nek9 by phosphorylation.The Journal of biological chemistry · 2013Article
- Multiple recognition motifs in nucleoporin Nup159 provide a stable and rigid Nup159-Dyn2 assembly.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Dynein light chain LC8 is a small, dimeric, and very highly conserved globular protein that is an integral part of the dynein and myosin molecular motors but appears to have a broader role in multiple protein complexes unrelated to molecular motors. LC8 binds to two families of targets: those having a KXTQT sequence fingerprint and those having a GIQVD fingerprint. All known LC8 binding partners containing these fingerprints share a common binding site on LC8 that raises the question of what determines binding specificity. Here, we present the crystal structure of apo-LC8 at 1.7-A resolution, which, when compared with the crystal structures of several LC8 complexes, gives insight into the mechanism underlying the binding diversity of LC8. Peptide binding is associated with a shift in quaternary structure that expands the hydrophobic binding surface available to the ligand, in addition to changes in tertiary structure and ordering of LC8 around the binding groove. The observed quaternary shift suggests a mechanism by which binding at one of the two identical sites can influence binding at the other. NMR spectra of titrations with peptides from each fingerprint family show evidence of allosteric interaction between the two binding sites, to a differing degree in the two ligand families. Allosteric interaction between the binding sites may be a mechanism to promote simultaneous binding of ligands from the same family, providing a physiological role for the two fingerprints.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.