scholarly journals Structure-based virtual screening for fragment-like ligands of the G protein-coupled histamine H4 receptor

MedChemComm ◽  
2015 ◽  
Vol 6 (6) ◽  
pp. 1003-1017 ◽  
Author(s):  
Enade P. Istyastono ◽  
Albert J. Kooistra ◽  
Henry F. Vischer ◽  
Martien Kuijer ◽  
Luc Roumen ◽  
...  
Keyword(s):  
Virtual Screening ◽  
G Protein ◽  
Histamine H4 Receptor ◽  
H4 Receptor ◽  
G Protein Coupled ◽  
Homology Models

Structure-based virtual screening using H1R- and β2R-based histamine H4R homology models identified 9 fragments with an affinity ranging from 0.14 to 6.3 μm for H4R.

scholarly journals Structure-Based Virtual Screening for Ligands of G Protein–Coupled Receptors: What Can Molecular Docking Do for You?

2021 ◽  
Vol 73 (4) ◽  
pp. 527-565
Author(s):  
Flavio Ballante ◽  
Albert J Kooistra ◽  
Stefanie Kampen ◽  
Chris de Graaf ◽  
Jens Carlsson
Keyword(s):  
Molecular Docking ◽  
Virtual Screening ◽  
G Protein ◽  
G Protein Coupled Receptors ◽  
G Protein Coupled

scholarly journals Enigmatic Histamine Receptor H4 for Potential Treatment of Multiple Inflammatory, Autoimmune, and Related Diseases

Life ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 50
Author(s):  
Pakhuri Mehta ◽  
Przemysław Miszta ◽  
Przemysław Rzodkiewicz ◽  
Olga Michalak ◽  
Piotr Krzeczyński ◽  
...  
Keyword(s):  
Cell Activation ◽  
Histamine Receptor ◽  
Mast Cell Activation ◽  
Histamine H4 Receptor ◽  
Inflammatory Models ◽  
The Family ◽  
Cellular Pathways ◽  
H4 Receptor ◽  
G Protein Coupled

The histamine H4 receptor, belonging to the family of G-protein coupled receptors, is an increasingly attractive drug target. It plays an indispensable role in many cellular pathways, and numerous H4R ligands are being studied for the treatment of several inflammatory, allergic, and autoimmune disorders, including pulmonary fibrosis. Activation of H4R is involved in cytokine production and mediates mast cell activation and eosinophil chemotaxis. The importance of this receptor has also been shown in inflammatory models: peritonitis, respiratory tract inflammation, colitis, osteoarthritis, and rheumatoid arthritis. Recent studies suggest that H4R acts as a modulator in cancer, neuropathic pain, vestibular disorders, and type-2 diabetes, however, its role is still not fully understood.

scholarly journals Modulating G-Protein Coupled Receptor/G-Protein Signal Transduction by Small Molecules Suggested by Virtual Screening

2008 ◽  
Vol 51 (17) ◽  
pp. 5297-5303 ◽  
Author(s):  
Christina M. Taylor ◽  
Yaniv Barda ◽  
Oleg G. Kisselev ◽  
Garland R. Marshall
Keyword(s):  
Signal Transduction ◽  
Virtual Screening ◽  
Small Molecules ◽  
G Protein ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

scholarly journals Locating ligand binding sites in G-protein coupled receptors using combined information from docking and sequence conservation

2018 ◽  
Author(s):  
Ashley R. Vidad ◽  
Stephen Macaspac ◽  
Ho-Leung Ng
Keyword(s):  
Ligand Binding ◽  
G Protein ◽  
Binding Sites ◽  
G Protein Coupled Receptors ◽  
Sequence Conservation ◽  
Surface Geometry ◽  
A2a Adenosine Receptors ◽  
Ligand Binding Sites ◽  
G Protein Coupled ◽  
Homology Models

AbstractG-protein coupled receptors (GPCRs) are the largest protein family of drug targets. Detailed mechanisms of binding are unknown for many important GPCR-ligand pairs due to the difficulties of GPCR recombinant expression, biochemistry, and crystallography. We describe our new method, ConDock, for predicting ligand binding sites in GPCRs using combined information from surface conservation and docking starting from crystal structures or homology models. We demonstrate the effectiveness of ConDock on well-characterized GPCRs such as the β2 adrenergic and A2A adenosine receptors. We also demonstrate that ConDock successfully predicts ligand binding sites from high-quality homology models. Finally, we apply ConDock to predict ligand binding sites on a structurally uncharacterized GPCR, GPER. GPER is the G-protein coupled estrogen receptor, with four known ligands: estradiol, G1, G15, and tamoxifen. ConDock predicts that all four ligands bind to the same location on GPER, centered on L119, H307, and N310; this site is deeper in the receptor cleft than predicted by previous studies. We compare the sites predicted by ConDock and traditional methods that utilize information from surface geometry, surface conservation, and ligand chemical interactions. Incorporating sequence conservation information in ConDock overcomes errors introduced from physics-based scoring functions and homology modeling.

scholarly journals Docking-based virtual screening for ligands of G protein-coupled receptors: Not only crystal structures but also in silico models

2011 ◽  
Vol 29 (5) ◽  
pp. 614-623 ◽  
Author(s):  
Santiago Vilar ◽  
Giulio Ferino ◽  
Sharangdhar S. Phatak ◽  
Barkin Berk ◽  
Claudio N. Cavasotto ◽  
...  
Keyword(s):  
Virtual Screening ◽  
Crystal Structures ◽  
G Protein ◽  
In Silico ◽  
G Protein Coupled Receptors ◽  
In Silico Models ◽  
G Protein Coupled

Discovery of Novel Human Histamine H4 Receptor Ligands by Large-Scale Structure-Based Virtual Screening

2008 ◽  
Vol 51 (11) ◽  
pp. 3145-3153 ◽  
Author(s):  
Róbert Kiss ◽  
Béla Kiss ◽  
Árpád Könczöl ◽  
Ferenc Szalai ◽  
Ivett Jelinek ◽  
...  
Keyword(s):  
Virtual Screening ◽  
Large Scale ◽  
Large Scale Structure ◽  
Scale Structure ◽  
Receptor Ligands ◽  
Histamine H4 Receptor ◽  
H4 Receptor ◽  
Human Histamine
Sign in / Sign up

Export Citation Format

Share Document