Rigidified Clicked Dimeric Ligands for Studying the Dynamics of the PDZ1-2 Supramodule of PSD-95

Department of Drug Design and Pharmacology

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Rigidified Clicked Dimeric Ligands for Studying the Dynamics of the PDZ1-2 Supramodule of PSD-95. / Eildal, Jonas N N; Bach, Anders; Dogan, Jakob; Ye, Fei; Zhang, Mingjie; Jemth, Per; Strømgaard, Kristian.

In: ChemBioChem, Vol. 16, 2015, p. 64–69.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Eildal, JNN, Bach, A, Dogan, J, Ye, F, Zhang, M, Jemth, P & Strømgaard, K 2015, 'Rigidified Clicked Dimeric Ligands for Studying the Dynamics of the PDZ1-2 Supramodule of PSD-95', ChemBioChem, vol. 16, pp. 64–69. https://doi.org/10.1002/cbic.201402547

APA

Eildal, J. N. N., Bach, A., Dogan, J., Ye, F., Zhang, M., Jemth, P., & Strømgaard, K. (2015). Rigidified Clicked Dimeric Ligands for Studying the Dynamics of the PDZ1-2 Supramodule of PSD-95. ChemBioChem, 16, 64–69. https://doi.org/10.1002/cbic.201402547

Vancouver

Eildal JNN, Bach A, Dogan J, Ye F, Zhang M, Jemth P et al. Rigidified Clicked Dimeric Ligands for Studying the Dynamics of the PDZ1-2 Supramodule of PSD-95. ChemBioChem. 2015;16:64–69. https://doi.org/10.1002/cbic.201402547

Author

Eildal, Jonas N N ; Bach, Anders ; Dogan, Jakob ; Ye, Fei ; Zhang, Mingjie ; Jemth, Per ; Strømgaard, Kristian. / Rigidified Clicked Dimeric Ligands for Studying the Dynamics of the PDZ1-2 Supramodule of PSD-95. In: ChemBioChem. 2015 ; Vol. 16. pp. 64–69.

Bibtex

@article{7f33f77c20c147eba46e37cb5b41e740,

title = "Rigidified Clicked Dimeric Ligands for Studying the Dynamics of the PDZ1-2 Supramodule of PSD-95",

abstract = "PSD-95 is a scaffolding protein of the MAGUK protein family, and engages in several vital protein-protein interactions in the brain with its PDZ domains. It has been suggested that PSD-95 is composed of two supramodules, one of which is the PDZ1-2 tandem domain. Here we have developed rigidified high-affinity dimeric ligands that target the PDZ1-2 supramodule, and established the biophysical parameters of the dynamic PDZ1-2/ligand interactions. By employing ITC, protein NMR, and stopped-flow kinetics this study provides a detailed insight into the overall conformational energetics of the interaction between dimeric ligands and tandem PDZ domains. Our findings expand our understanding of the dynamics of PSD-95 with potential relevance to its biological role in interacting with multivalent receptor complexes and development of novel drugs.",

author = "Eildal, {Jonas N N} and Anders Bach and Jakob Dogan and Fei Ye and Mingjie Zhang and Per Jemth and Kristian Str{\o}mgaard",

note = "{\textcopyright} 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",

year = "2015",

doi = "10.1002/cbic.201402547",

language = "English",

volume = "16",

pages = "64–69",

journal = "ChemBioChem",

issn = "1439-4227",

publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",

}

RIS

TY - JOUR

T1 - Rigidified Clicked Dimeric Ligands for Studying the Dynamics of the PDZ1-2 Supramodule of PSD-95

AU - Eildal, Jonas N N

AU - Bach, Anders

AU - Dogan, Jakob

AU - Ye, Fei

AU - Zhang, Mingjie

AU - Jemth, Per

AU - Strømgaard, Kristian

PY - 2015

Y1 - 2015

N2 - PSD-95 is a scaffolding protein of the MAGUK protein family, and engages in several vital protein-protein interactions in the brain with its PDZ domains. It has been suggested that PSD-95 is composed of two supramodules, one of which is the PDZ1-2 tandem domain. Here we have developed rigidified high-affinity dimeric ligands that target the PDZ1-2 supramodule, and established the biophysical parameters of the dynamic PDZ1-2/ligand interactions. By employing ITC, protein NMR, and stopped-flow kinetics this study provides a detailed insight into the overall conformational energetics of the interaction between dimeric ligands and tandem PDZ domains. Our findings expand our understanding of the dynamics of PSD-95 with potential relevance to its biological role in interacting with multivalent receptor complexes and development of novel drugs.

AB - PSD-95 is a scaffolding protein of the MAGUK protein family, and engages in several vital protein-protein interactions in the brain with its PDZ domains. It has been suggested that PSD-95 is composed of two supramodules, one of which is the PDZ1-2 tandem domain. Here we have developed rigidified high-affinity dimeric ligands that target the PDZ1-2 supramodule, and established the biophysical parameters of the dynamic PDZ1-2/ligand interactions. By employing ITC, protein NMR, and stopped-flow kinetics this study provides a detailed insight into the overall conformational energetics of the interaction between dimeric ligands and tandem PDZ domains. Our findings expand our understanding of the dynamics of PSD-95 with potential relevance to its biological role in interacting with multivalent receptor complexes and development of novel drugs.

U2 - 10.1002/cbic.201402547

DO - 10.1002/cbic.201402547

M3 - Journal article

C2 - 25407949

VL - 16

SP - 64

EP - 69

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

ER -

ID: 127818544