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Je něco špatně v tomto záznamu ?
Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences
K. Melková, V. Zapletal, S. Narasimhan, S. Jansen, J. Hritz, R. Škrabana, M. Zweckstetter, M. Ringkjøbing Jensen, M. Blackledge, L. Žídek,
Jazyk angličtina Země Švýcarsko
Typ dokumentu časopisecké články, práce podpořená grantem, přehledy
NLK
Directory of Open Access Journals
od 2011
PubMed Central
od 2011
Europe PubMed Central
od 2011
ProQuest Central
od 2011-01-01
Open Access Digital Library
od 2011-01-01
Open Access Digital Library
od 2011-01-01
Health & Medicine (ProQuest)
od 2011-01-01
ROAD: Directory of Open Access Scholarly Resources
od 2011
PubMed
30884818
DOI
10.3390/biom9030105
Knihovny.cz E-zdroje
- MeSH
- lidé MeSH
- mikrotubuly chemie metabolismus MeSH
- proteiny asociované s mikrotubuly chemie metabolismus MeSH
- proteiny tau chemie metabolismus MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
The stability and dynamics of cytoskeleton in brain nerve cells are regulated by microtubule associated proteins (MAPs), tau and MAP2. Both proteins are intrinsically disordered and involved in multiple molecular interactions important for normal physiology and pathology of chronic neurodegenerative diseases. Nuclear magnetic resonance and cryo-electron microscopy recently revealed propensities of MAPs to form transient local structures and long-range contacts in the free state, and conformations adopted in complexes with microtubules and filamentous actin, as well as in pathological aggregates. In this paper, we compare the longest, 441-residue brain isoform of tau (tau40), and a 467-residue isoform of MAP2, known as MAP2c. For both molecules, we present transient structural motifs revealed by conformational analysis of experimental data obtained for free soluble forms of the proteins. We show that many of the short sequence motifs that exhibit transient structural features are linked to functional properties, manifested by specific interactions. The transient structural motifs can be therefore classified as molecular recognition elements of tau40 and MAP2c. Their interactions are further regulated by post-translational modifications, in particular phosphorylation. The structure-function analysis also explains differences between biological activities of tau40 and MAP2c.
Citace poskytuje Crossref.org
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- $a Melková, Kateřina $u Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. katerina.melkova@ceitec.muni.cz. Faculty of Science, National Centre for Biomolecular Research, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. katerina.melkova@ceitec.muni.cz.
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- $a Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences / $c K. Melková, V. Zapletal, S. Narasimhan, S. Jansen, J. Hritz, R. Škrabana, M. Zweckstetter, M. Ringkjøbing Jensen, M. Blackledge, L. Žídek,
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- $a The stability and dynamics of cytoskeleton in brain nerve cells are regulated by microtubule associated proteins (MAPs), tau and MAP2. Both proteins are intrinsically disordered and involved in multiple molecular interactions important for normal physiology and pathology of chronic neurodegenerative diseases. Nuclear magnetic resonance and cryo-electron microscopy recently revealed propensities of MAPs to form transient local structures and long-range contacts in the free state, and conformations adopted in complexes with microtubules and filamentous actin, as well as in pathological aggregates. In this paper, we compare the longest, 441-residue brain isoform of tau (tau40), and a 467-residue isoform of MAP2, known as MAP2c. For both molecules, we present transient structural motifs revealed by conformational analysis of experimental data obtained for free soluble forms of the proteins. We show that many of the short sequence motifs that exhibit transient structural features are linked to functional properties, manifested by specific interactions. The transient structural motifs can be therefore classified as molecular recognition elements of tau40 and MAP2c. Their interactions are further regulated by post-translational modifications, in particular phosphorylation. The structure-function analysis also explains differences between biological activities of tau40 and MAP2c.
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- $a Zapletal, Vojtěch $u Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. vojtech.zapletal@ceitec.muni.cz. Faculty of Science, National Centre for Biomolecular Research, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. vojtech.zapletal@ceitec.muni.cz.
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- $a Zweckstetter, Markus $u German Center for Neurodegenerative Diseases (DZNE), Von-Siebold-Str. 3a, 37075 Göttingen, Germany. Markus.Zweckstetter@dzne.de. Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany. Markus.Zweckstetter@dzne.de.
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- $a Žídek, Lukáš $u Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. lzidek@chemi.muni.cz. Faculty of Science, National Centre for Biomolecular Research, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic. lzidek@chemi.muni.cz.
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