scholarly journals Importance of Homology Modeling for Predicting the Structures of GPCRs

2020 ◽  
Author(s):  
Ananthasri Sailapathi ◽  
Seshan Gunalan ◽  
Kanagasabai Somarathinam ◽  
Gugan Kothandan ◽  
Diwakar Kumar

Homology modeling is one of the key discoveries that led to a rapid paradigm shift in the field of computational biology. Homology modeling obtains the three dimensional structure of a target protein based on the similarity between template and target sequences and this technique proves to be efficient when it comes to studying membrane proteins that are hard to crystallize like GPCR as it provides a higher degree of understanding of receptor-ligand interaction. We get profound insights on structurally unsolved, yet clinically important drug targeting proteins through single or multiple template modeling. The advantages of homology modeling studies are often used to overcome various problems in crystallizing GPCR proteins that are involved in major disease-related pathways, thus paving way to more structural insights via in silico models when there is a lack of experimentally solved structures. Owing to their pharmaceutical significance, structural analysis of various GPCR proteins using techniques like homology modeling is of utmost importance.

2006 ◽  
Vol 72 (4) ◽  
pp. 3021-3025 ◽  
Author(s):  
Jin-Kyu Rhee ◽  
Do-Yun Kim ◽  
Dae-Gyun Ahn ◽  
Jung-Hyuk Yun ◽  
Seung-Hwan Jang ◽  
...  

ABSTRACT The three-dimensional (3D) structure of the hyperthermophilic esterase EstE1 was constructed by homology modeling using Archaeoglobus fulgidus esterase as a reference, and the thermostability-structure relationship was analyzed. Our results verified the predicted 3D structure of EstE1 and identified the ion pair networks and hydrophobic interactions that are critical determinants for the thermostability of EstE1.


1996 ◽  
Vol 9 (6) ◽  
pp. 493-498 ◽  
Author(s):  
Romano T. Kroemer ◽  
Stephen W. Doughty ◽  
Alan J. Robinson ◽  
W. Graham Richards

1993 ◽  
Vol 98 (D11) ◽  
pp. 20685 ◽  
Author(s):  
Kwo-Sen Kuo ◽  
Ronald M. Welch ◽  
Ronald C. Weger ◽  
Mark A. Engelstad ◽  
S. K. Sengupta

1970 ◽  
Vol 1 (2) ◽  
pp. 18-26 ◽  
Author(s):  
Md Musharaf Hossain

Antifreeze proteins (AFPs) protect organisms from freezing and shows great diversity in structure, and they have been found in a variety of organisms. In this study, a total of 15 antifreeze proteins of fish were selected where they represent distinct physicochemical and structural features. The present paper uses bioinformatics approach to describe the physiochemical, functional and structural properties of Antifreeze proteins. Several Physico-chemical properties such as pI, EC, AI, GRAVY and instability index are computed and provide data about these proteins and their properties. The result of primary structure analysis infers that, fish antifreeze proteins are mostly hydrophobic. Disulfide bridges and secondary structures were analyzed using CYS_REC and SOPMA respectively. The three dimensional structure of Antifreeze proteins is predicted by using three homology modeling server Geno3D, Swiss-model and CPHmodels. The model was evaluated with PROCHECK, WHAT IF, and ProSA programs. Model visualization and analysis was done with Pymol. These structures will provide a good foundation for functional analysis of experimentally derived crystal structures.Key Words: Antifreeze Proteins; Computational tools; hydrophobicity; homology modeling; isoelectric point.DOI: http://dx.doi.org/10.3329/icpj.v1i2.9412International Current Pharmaceutical Journal 2012, 1(2): 18-26


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