Silico docking studies of ITPA mutants: the analysis of protein-ligand interactions
Faculty Mentor
Yao Houndonougbo
Document Type
Poster
Start Date
10-5-2023 11:15 AM
End Date
10-5-2023 1:00 PM
Location
PUB NCR
Department
Chemistry and Biochemistry
Abstract
Inosine triphosphate pyrophosphatase, also known as ITPA is an enzyme that plays an important role by preventing genetic instability. As proteins are built, non-canonical purines are made within the nucleotide base pairing that deviate from the standard set by Watson and Crick. ITPA is bound to Inosine Triphosphate (ITP) and ITPA-ITP complex provides genomic stability by hydrolyzing inosine triphosphate to a monophosphate nucleotide and deoxyinosine triphosphate to diphosphate which prevents genetic abnormality within our DNA/RNA. A common mutation in human ITPA is the proline to threonine substitution at position 32. About 15% of the world’s population possesses the ITPA P32T mutant which is linked to poor outcomes in thiopurine drug therapy for autoimmune diseases, inflammatory bowel disease, and acute lymphoblastic leukemia. In silico docking method is widely used to study protein-ligand interactions which are important for understanding the mechanisms of biological regulation. In this study, we used Autodock 4 software to predict P32T-ITP complex. We report the binding energies and the similarity of the docked structures. The study provides the basis for understanding P32T-ITP interactions.
Recommended Citation
Cardenas, Jenna, "Silico docking studies of ITPA mutants: the analysis of protein-ligand interactions" (2023). 2023 Symposium. 9.
https://dc.ewu.edu/srcw_2023/res_2023/p2_2023/9
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
Silico docking studies of ITPA mutants: the analysis of protein-ligand interactions
PUB NCR
Inosine triphosphate pyrophosphatase, also known as ITPA is an enzyme that plays an important role by preventing genetic instability. As proteins are built, non-canonical purines are made within the nucleotide base pairing that deviate from the standard set by Watson and Crick. ITPA is bound to Inosine Triphosphate (ITP) and ITPA-ITP complex provides genomic stability by hydrolyzing inosine triphosphate to a monophosphate nucleotide and deoxyinosine triphosphate to diphosphate which prevents genetic abnormality within our DNA/RNA. A common mutation in human ITPA is the proline to threonine substitution at position 32. About 15% of the world’s population possesses the ITPA P32T mutant which is linked to poor outcomes in thiopurine drug therapy for autoimmune diseases, inflammatory bowel disease, and acute lymphoblastic leukemia. In silico docking method is widely used to study protein-ligand interactions which are important for understanding the mechanisms of biological regulation. In this study, we used Autodock 4 software to predict P32T-ITP complex. We report the binding energies and the similarity of the docked structures. The study provides the basis for understanding P32T-ITP interactions.
