ArticleJournal of biomolecular NMR2002
Backbone dynamics of the 8 kDa dynein light chain dimer reveals molecular basis of the protein's functional diversity.
Article in Journal of biomolecular NMR, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Systematic identification of recognition motifs for the hub protein LC8.Life science alliance · 2019Article
- 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
- Resonance Assignments and Secondary Structure Analysis of Dynein Light Chain 8 by Magic Angle Spinning NMR Spectroscopy.Canadian journal of chemistry · 2011Article
- Affinity, avidity, and kinetics of target sequence binding to LC8 dynein light chain isoforms.The Journal of biological chemistry · 2010Article
- Structure-function-folding relationships and native energy landscape of dynein light chain protein: nuclear magnetic resonance insights.Journal of biosciences · 2009Review
- The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8.Journal of molecular biology · 2008Article
- pH driven conformational dynamics and dimer-to-monomer transition in DLC8.Protein science : a publication of the Protein Society · 2006Article
- Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands.The Biochemical journal · 2004Article
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Authors and funding
4 authors.
Funding
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Abstract
Axonemal and cytoplasmic dyneins share a highly conserved 8 kDa light chain (DLC8) for motor assembly and function. Other than serving as a light chain of dynein complexes, DLC8 has been shown to bind a larger number of proteins with diverse biological functions including cell cycle control, apoptosis, and cell polarity maintenance. Therefore, DLC8 is likely a multifunctional regulatory protein. DLC8 exists as a dimer in solution, and the protein dimer is capable of binding to two target molecules. In this work, the backbone dynamics of DLC8, both in its apo- and target-peptide bound forms, were characterized by 15N NMR relaxation studies. The relaxation data were analyzed using model-free approach. We show that the target peptide-binding region of apo-DLC8 experiences microsecond-to-millisecond time scale conformational fluctuation, suggesting that the target-binding region of the protein is capable of adjusting its shape and size in responding to its various targets. The conformational breathing of the target-binding region of apo-DLC8 was also supported by backbone amide exchange experiment. Such segmental conformational motion of the protein is significantly reduced upon forming a complex with a target peptide. The dynamic properties of DLC8 in solution provide insight into the protein's diverse sequence-dependent target binding.
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Registered trials
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