Conformational Selection of Dimethylarginine Recognition by the
Survival Motor Neuron Tudor Domain

J 2018

Conformational Selection of Dimethylarginine Recognition by the Survival Motor Neuron Tudor Domain

SUPEKAR, S.; Anna PAPAGEORGIOU; G. GEMMECKER; R. PELTZER; M.P. JOHANSSON et. al.

Basic information

Original name

Conformational Selection of Dimethylarginine Recognition by the Survival Motor Neuron Tudor Domain

Authors

SUPEKAR, S. (276 Germany); Anna PAPAGEORGIOU (300 Greece, belonging to the institution); G. GEMMECKER (276 Germany); R. PELTZER (276 Germany); M.P. JOHANSSON (578 Norway); Konstantinos TRIPSIANES (300 Greece, guarantor, belonging to the institution); M. SATTLER (276 Germany) and V.R.I. KAILA (276 Germany)

Edition

Angewandte Chemie International Edition, WEINHEIM (GERMANY), Verlag Chemie, 2018, 1433-7851

Other information

Language

English

Type of outcome

Article in a journal

Field of Study

10402 Inorganic and nuclear chemistry

Country of publisher

Germany

Confidentiality degree

is not subject to a state or trade secret

Impact factor

Impact factor: 12.257

RIV identification code

RIV/00216224:14740/18:00101121

Organization unit

Central European Institute of Technology

DOI

https://doi.org/10.1002/anie.201708233

UT WoS

000419110500018

EID Scopus

2-s2.0-85042112129

Keywords in English

arginine rotation; cation-p interactions; dynamic NMR; QM/MM; quantum chemistry

Abstract

In the original language

Tudor domains bind to dimethylarginine (DMA) residues, which are post-translational modifications that play a central role in gene regulation in eukaryotic cells. NMR spectroscopy and quantum calculations are combined to demonstrate that DMA recognition by Tudor domains involves conformational selection. The binding mechanism is confirmed by a mutation in the aromatic cage that perturbs the native recognition mode of the ligand. General mechanistic principles are delineated from the combined results, indicating that Tudor domains utilize cation-p interactions to achieve ligand recognition.

Links

GJ15-22380Y, research and development project

Name: Molekulární stavba protein-DNA komplexů zapojených v opravě nukleotidových sestřihů

Investor: Czech Science Foundation

LQ1601, research and development project

Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR

Cite

SUPEKAR, S.; Anna PAPAGEORGIOU; G. GEMMECKER; R. PELTZER; M.P. JOHANSSON; Konstantinos TRIPSIANES; M. SATTLER and V.R.I. KAILA. Conformational Selection of Dimethylarginine Recognition by the Survival Motor Neuron Tudor Domain. Angewandte Chemie International Edition. WEINHEIM (GERMANY): Verlag Chemie, 2018, vol. 57, No 2, p. 486-490. ISSN 1433-7851. Available from: https://doi.org/10.1002/anie.201708233.

@article{1430704,
   author = {Supekar, S. and Papageorgiou, Anna and Gemmecker, G. and Peltzer, R. and Johansson, M.P. and Tripsianes, Konstantinos and Sattler, M. and Kaila, V.R.I.},
   article_location = {WEINHEIM (GERMANY)},
   article_number = {2},
   doi = {https://doi.org/10.1002/anie.201708233},
   keywords = {arginine rotation; cation-p interactions; dynamic NMR; QM/MM; quantum chemistry},
   language = {eng},
   issn = {1433-7851},
   journal = {Angewandte Chemie International Edition},
   title = {Conformational Selection of Dimethylarginine Recognition by the Survival Motor Neuron Tudor Domain},
   volume = {57},
   year = {2018}
}

TY  - JOUR
ID  - 1430704
AU  - Supekar, S. - Papageorgiou, Anna - Gemmecker, G. - Peltzer, R. - Johansson, M.P. - Tripsianes, Konstantinos - Sattler, M. - Kaila, V.R.I.
PY  - 2018
TI  - Conformational Selection of Dimethylarginine Recognition by the Survival Motor Neuron Tudor Domain
JF  - Angewandte Chemie International Edition
VL  - 57
IS  - 2
SP  - 486-490
EP  - 486-490
PB  - Verlag Chemie
SN  - 14337851
KW  - arginine rotation
KW  - cation-p interactions
KW  - dynamic NMR
KW  - QM/MM
KW  - quantum chemistry
N2  - Tudor domains bind to dimethylarginine (DMA) residues, which are post-translational modifications that play a central role in gene regulation in eukaryotic cells. NMR spectroscopy and quantum calculations are combined to demonstrate that DMA recognition by Tudor domains involves conformational selection. The binding mechanism is confirmed by a mutation in the aromatic cage that perturbs the native recognition mode of the ligand. General mechanistic principles are delineated from the combined results, indicating that Tudor domains utilize cation-p interactions to achieve ligand recognition.
ER  -

SUPEKAR, S.; Anna PAPAGEORGIOU; G. GEMMECKER; R. PELTZER; M.P. JOHANSSON; Konstantinos TRIPSIANES; M. SATTLER and V.R.I. KAILA. Conformational Selection of Dimethylarginine Recognition by the Survival Motor Neuron Tudor Domain. \textit{Angewandte Chemie International Edition}. WEINHEIM (GERMANY): Verlag Chemie, 2018, vol.~57, No~2, p.~486-490. ISSN~1433-7851. Available from: https://doi.org/10.1002/anie.201708233.

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