ZAPLETAL, Vojtěch, Kateřina MELKOVÁ, Séverine JANSEN, Erik NOMILNER, M.R. JENSEN, M. BLACKLEDGE and Lukáš ŽÍDEK. Conformation and dynamics of intrinsically disordered microtubule associated protein 2c. 2018. ISSN 2211-5463. Available from: https://dx.doi.org/10.1002/2211-5463.12453.
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Basic information
Original name Conformation and dynamics of intrinsically disordered microtubule associated protein 2c
Authors ZAPLETAL, Vojtěch (203 Czech Republic, belonging to the institution), Kateřina MELKOVÁ (203 Czech Republic, belonging to the institution), Séverine JANSEN (250 France, belonging to the institution), Erik NOMILNER (703 Slovakia, belonging to the institution), M.R. JENSEN (250 France), M. BLACKLEDGE (250 France) and Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution).
Edition 2018.
Other information
Original language English
Type of outcome Conference abstract
Field of Study 10608 Biochemistry and molecular biology
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 1.959
RIV identification code RIV/00216224:14740/18:00103544
Organization unit Central European Institute of Technology
ISSN 2211-5463
Doi http://dx.doi.org/10.1002/2211-5463.12453
UT WoS 000437674104279
Keywords in English protein 2c; MAP2c
Tags rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 26/3/2019 15:24.
Abstract
Microtubule associated protein 2c (MAP2c) regulates structure and dynamics (polymerization and degradation) of microtubules in developing neurons and other cells. MAP2c is a 49 kDa intrinsically disordered protein (IDP) consisting of several structural and functional regions. The N-terminal part contains two important regions: An N-terminal region with a high content of negatively charged amino acids and a proline-rich region. The former segment contains a binding site for the regulatory subunit of cAMP-dependent protein kinase (PKA) and proposed binding site for steroids, while the latter one contains several phosphorylation sites. The second important part of MAP2c is a highlyconserved C-terminal domain that binds to microtubules. In order to investigate relation between highly dynamic structural features of MAP2c and its functions, we studied dynamics of MAP2c using nuclear magnetic resonance (NMR) relaxation and performed quantitative conformational analysis of NMR chemical shifts, small angle X-ray scattering, and paramagnetic relaxation enhancement. Pools of possible chain conformations were generated by the program Flexible-Meccano, which builds consecutively a polypeptide chain. The ensemble of structures reproducing the experimental data was selected by the program ASTEROIDS which uses a genetic algorithm. We found out that the least flexible amino acids are involved in transient long-range contacts between the acidic N-terminal domain and the microtubule-binding domain and that more ordered regions correlate with the regions of known or proposed function. Our results thus indicate importance of the N-terminal regions for the specificity of regulatory roles of MAP2c and a close relation between biological functions and conformational behavior of this protein
Abstract (in Czech)
Microtubule associated protein 2c (MAP2c) regulates structure and dynamics (polymerization and degradation) of microtubules in developing neurons and other cells. MAP2c is a 49 kDa intrinsically disordered protein (IDP) consisting of several structural and functional regions. The N-terminal part contains two important regions: An N-terminal region with a high content of negatively charged amino acids and a proline-rich region. The former segment contains a binding site for the regulatory subunit of cAMP-dependent protein kinase (PKA) and proposed binding site for steroids, while the latter one contains several phosphorylation sites. The second important part of MAP2c is a highlyconserved C-terminal domain that binds to microtubules. In order to investigate relation between highly dynamic structural features of MAP2c and its functions, we studied dynamics of MAP2c using nuclear magnetic resonance (NMR) relaxation and performed quantitative conformational analysis of NMR chemical shifts, small angle X-ray scattering, and paramagnetic relaxation enhancement. Pools of possible chain conformations were generated by the program Flexible-Meccano, which builds consecutively a polypeptide chain. The ensemble of structures reproducing the experimental data was selected by the program ASTEROIDS which uses a genetic algorithm. We found out that the least flexible amino acids are involved in transient long-range contacts between the acidic N-terminal domain and the microtubule-binding domain and that more ordered regions correlate with the regions of known or proposed function. Our results thus indicate importance of the N-terminal regions for the specificity of regulatory roles of MAP2c and a close relation between biological functions and conformational behavior of this protein
Links
LQ1601, research and development projectName: CEITEC 2020 (Acronym: CEITEC2020)
Investor: Ministry of Education, Youth and Sports of the CR
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