ArticleJournal of molecular biology2013
Three-dimensional structure of CAP-gly domain of mammalian dynactin determined by magic angle spinning NMR spectroscopy: conformational plasticity and interactions with end-binding protein EB1.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Improved Protocol for the Production of the Low-Expression Eukaryotic Membrane Protein Human Aquaporin 2 inBiomolecules · 2020Article
- Conformational Flexibility of p150Biophysical journal · 2019Article
- Accuracy and precision of protein structures determined by magic angle spinning NMR spectroscopy: for some 'with a little help from a friend'.Journal of biomolecular NMR · 2019Article
- Backbone amideSolid state nuclear magnetic resonance · 2018Article
- Detecting and accounting for multiple sources of positional variance in peak list registration analysis and spin system grouping.Journal of biomolecular NMR · 2017Article
- Mapping protein-protein interactions by double-REDOR-filtered magic angle spinning NMR spectroscopy.Journal of biomolecular NMR · 2017Article
- Dynactin has two antagonistic regulatory domains and exerts opposing effects on dynein motility.PloS one · 2017Article
- Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Quarterly reviews of biophysics · 2017Review
- Atomic-resolution structure of the CAP-Gly domain of dynactin on polymeric microtubules determined by magic angle spinning NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Internal dynamics of dynactin CAP-Gly is regulated by microtubules and plus end tracking protein EB1.The Journal of biological chemistry · 2015Article
- Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment.Journal of biomolecular NMR · 2014Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Microtubules and their associated proteins play important roles in vesicle and organelle transport, cell motility and cell division. Perturbation of these processes by mutation typically gives rise to severe pathological conditions. In our efforts to obtain atomic information on microtubule-associated protein/microtubule interactions with the goal to understand mechanisms that might potentially assist in the development of treatments for these diseases, we have determined the three-dimensional structure of CAP-Gly (cytoskeleton-associated protein, glycine-rich) domain of mammalian dynactin by magic angle spinning NMR spectroscopy. We observe two conformations in the β2 strand encompassing residues T43-V44-A45, residues that are adjacent to the disease-associated mutation, G59S. Upon binding of CAP-Gly to microtubule plus-end tracking protein EB1, the CAP-Gly shifts to a single conformer. We find extensive chemical shift perturbations in several stretches of residues of CAP-Gly upon binding to EB1, from which we define accurately the CAP-Gly/EB1 binding interface. We also observe that the loop regions may exhibit unique flexibility, especially in the GKNDG motif, which participates in the microtubule binding. This study in conjunction with our previous reports suggests that conformational plasticity is an intrinsic property of CAP-Gly likely due to its unusually high loop content and may be required for its biological functions.
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