NMR Chemical Shift Perturbation Study of the N-Terminal Domain of Hsp90 upon Binding of ADP, AMP-PNP, Geldanamycin, and Radicicol

ChemBioChem ◽  
2003 ◽  
Vol 4 (9) ◽  
pp. 870-877 ◽  
Author(s):  
Alexander Dehner ◽  
Julien Furrer ◽  
Klaus Richter ◽  
Ioana Schuster ◽  
Johannes Buchner ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Chemical Shift Perturbation ◽  
Nmr Chemical Shift ◽  
Terminal Domain

scholarly journals Interactions between Human Liver Fatty Acid Binding Protein and Peroxisome Proliferator Activated Receptor Selective Drugs

PPAR Research ◽  
2013 ◽  
Vol 2013 ◽  
pp. 1-14 ◽  
Author(s):  
Tony Velkov
Keyword(s):  
Fatty Acid ◽  
Chemical Shift ◽  
Conformational Changes ◽  
Gene Activation ◽  
Chemical Shift Perturbation ◽  
Peroxisome Proliferator ◽  
Nmr Chemical Shift ◽  
Fatty Acid Binding ◽  
Regulatory Pathways ◽  
Subtype Selective

Fatty acid binding proteins (FABPs) act as intracellular shuttles for fatty acids as well as lipophilic xenobiotics to the nucleus, where these ligands are released to a group of nuclear receptors called the peroxisome proliferator activated receptors (PPARs). PPAR mediated gene activation is ultimately involved in maintenance of cellular homeostasis through the transcriptional regulation of metabolic enzymes and transporters that target the activating ligand. Here we show that liver- (L-) FABP displays a high binding affinity for PPAR subtype selective drugs. NMR chemical shift perturbation mapping and proteolytic protection experiments show that the binding of the PPAR subtype selective drugs produces conformational changes that stabilize the portal region of L-FABP. NMR chemical shift perturbation studies also revealed that L-FABP can form a complex with the PPAR ligand binding domain (LBD) of PPARα. This protein-protein interaction may represent a mechanism for facilitating the activation of PPAR transcriptional activity via the direct channeling of ligands between the binding pocket of L-FABP and the PPARαLBD. The role of L-FABP in the delivery of ligands directly to PPARαvia this channeling mechanism has important implications for regulatory pathways that mediate xenobiotic responses and host protection in tissues such as the small intestine and the liver where L-FABP is highly expressed.

scholarly journals Chemical shift assignments of the N-terminal domain of PSD95 (PSD95-NT)

2021 ◽  
Author(s):  
Yonghong Zhang ◽  
Johannes W. Hell ◽  
James B. Ames
Keyword(s):  
Synaptic Plasticity ◽  
Chemical Shift ◽  
Glutamate Receptors ◽  
Postsynaptic Density ◽  
Chemical Shift Assignments ◽  
Nmr Chemical Shift ◽  
Target Proteins ◽  
Terminal Domain ◽  
Neuronal Synapses ◽  
Nmr Chemical Shift Assignments

AbstractPostsynaptic density protein-95 (PSD95) contributes to the postsynaptic architecture of neuronal synapses and plays an important role in controlling synaptic plasticity. The N-terminal domain of PSD95 (residues 1–71, called PSD95-NT) interacts with target proteins (calmodulin, α-actinin-1 and CDKL5), which regulate the Ca2+-dependent degradation of glutamate receptors. We report complete backbone NMR chemical shift assignments of PSD95-NT (BMRB No. 50752).

Ubiquitin Binding Interface Mapping on Yeast Ubiquitin Hydrolase by NMR Chemical Shift Perturbation†

Biochemistry ◽  
1999 ◽  
Vol 38 (29) ◽  
pp. 9242-9253 ◽  
Author(s):  
Sundaresan Rajesh ◽  
Taiichi Sakamoto ◽  
Mariko Iwamoto-Sugai ◽  
Takehiko Shibata ◽  
Toshiyuki Kohno ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Chemical Shift Perturbation ◽  
Nmr Chemical Shift ◽  
Binding Interface ◽  
Ubiquitin Binding
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