In silicoanalysis of human Toll-like receptor 7 ligand binding domain

2015 ◽  
Vol 63 (3) ◽  
pp. 441-450 ◽  
Author(s):  
Chhedi Lal Gupta ◽  
Salman Akhtar ◽  
Uzma Sayyed ◽  
Neelam Pathak ◽  
Preeti Bajpai
Keyword(s):  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Toll Like Receptor

scholarly journals The molecular structure of the Toll-like receptor 3 ligand-binding domain

2005 ◽  
Vol 102 (31) ◽  
pp. 10976-10980 ◽  
Author(s):  
J. K. Bell ◽  
I. Botos ◽  
P. R. Hall ◽  
J. Askins ◽  
J. Shiloach ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Toll Like Receptor

Exploration of the peptide ligand-binding domain of the motilin receptor using photoaffinity labeling and receptor mutagenesis

2001 ◽  
Vol 120 (5) ◽  
pp. A509-A509
Author(s):  
B MATSUURA ◽  
M DONG ◽  
B COULIE ◽  
E HADAC ◽  
D PINON ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Photoaffinity Labeling ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Peptide Ligand ◽  
Motilin Receptor

Distinct Modulation of Wild-Type and Selective Gene Mutated Vitamin D Receptor by Essential Poly Unsaturated Fatty Acids

2021 ◽  
Vol 21 ◽  
Author(s):  
Hari Balaji ◽  
Selvaraj Ayyamperuma ◽  
Niladri Saha ◽  
Shyam Sundar Pottabathula ◽  
Jubie Selvaraj ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Vitamin D ◽  
Ligand Binding ◽  
Vitamin D Deficiency ◽  
Binding Affinity ◽  
Unsaturated Fatty Acids ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Binding Energies ◽  
Wild Type

: Vitamin-D deficiency is a global concern. Gene mutations in the vitamin D receptor’s (VDR) ligand binding domain (LBD) variously alter the ligand binding affinity, heterodimerization with retinoid X receptor (RXR) and inhibit coactivator interactions. These LBD mutations may result in partial or total hormone unresponsiveness. A plethora of evidence report that selective long chain polyunsaturated fatty acids (PUFAs) including eicosapentaenoic acid (EPA), docosahexaenoic acid (DHA) and arachidonic acid (AA) bind to the ligand-binding domain of VDR and lead to transcriptional activation. We therefore hypothesize that selective PUFAs would modulate the dynamics and kinetics of VDRs, irrespective bioactive of vitamin-D binding. The spatial arrangements of the selected PUFAs in VDR active site were examined by in-silico docking studies. The docking results revealed that PUFAs have fatty acid structure-specific binding affinity towards VDR. The calculated EPA, DHA & AA binding energies (Cdocker energy) were lesser compared to vitamin-D in wild type of VDR (PDB id: 2ZLC). Of note, the DHA has higher binding interactions to the mutated VDR (PDB id: 3VT7) when compared to the standard Vitamin-D. Molecular dynamic simulation was utilized to confirm the stability of potential compound binding of DHA with mutated VDR complex. These findings suggest the unique roles of PUFAs in VDR activation and may offer alternate strategy to circumvent vitamin-D deficiency.

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