ZAPLETAL, Vojtěch, Kateřina MELKOVÁ, Séverine JANSEN, Erik NOMILNER, M.R. JENSEN, M. BLACKLEDGE a Lukáš ŽÍDEK. Conformation and dynamics of intrinsically disordered microtubule associated protein 2c. ISSN 2211-5463. doi:10.1002/2211-5463.12453. 2018.
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Základní údaje
Originální název Conformation and dynamics of intrinsically disordered microtubule associated protein 2c
Autoři ZAPLETAL, Vojtěch (203 Česká republika, domácí), Kateřina MELKOVÁ (203 Česká republika, domácí), Séverine JANSEN (250 Francie, domácí), Erik NOMILNER (703 Slovensko, domácí), M.R. JENSEN (250 Francie), M. BLACKLEDGE (250 Francie) a Lukáš ŽÍDEK (203 Česká republika, garant, domácí).
Vydání 2018.
Další údaje
Originální jazyk angličtina
Typ výsledku Konferenční abstrakt
Obor 10608 Biochemistry and molecular biology
Stát vydavatele Spojené státy
Utajení není předmětem státního či obchodního tajemství
WWW URL
Impakt faktor Impact factor: 1.959
Kód RIV RIV/00216224:14740/18:00103544
Organizační jednotka Středoevropský technologický institut
ISSN 2211-5463
Doi http://dx.doi.org/10.1002/2211-5463.12453
UT WoS 000437674104279
Klíčová slova anglicky protein 2c; MAP2c
Štítky rivok
Příznaky Mezinárodní význam, Recenzováno
Změnil Změnila: Mgr. Pavla Foltynová, Ph.D., učo 106624. Změněno: 26. 3. 2019 15:24.
Anotace
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
Anotace česky
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
Návaznosti
LQ1601, projekt VaVNázev: CEITEC 2020 (Akronym: CEITEC2020)
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020
VytisknoutZobrazeno: 29. 3. 2024 00:53