- Tytuł:
- Docking for drug interface residues of modelled VPS33B of human with PtpA of Mycobacterium tuberculosis CDC1551
- Autorzy:
-
Reddy, K.M.
Pattathil, M.D.
Jayachandra, S.Y.
Parameshwar, A.
Sulochana, M.B. - Powiązania:
- https://bibliotekanauki.pl/articles/11443.pdf
- Data publikacji:
- 2014
- Wydawca:
- Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
- Tematy:
-
antigenicity
protein-protein interaction
network
homology modelling
drug design
interface residue
Mycobacterium tuberculosis
man
protein
biological function - Opis:
- VPS33B, a human Vacuolar Protein Sorting (VPS) protein which mediates the phagolysosomal fusion in macrophage of the eukaryotic organisms. This protein has a great role during the mycobacterial infections, which binds with the Mycobacterium protein tyrosine phosphatase A (PtpA). A single functional domain of PtpA has been identified using SMART domain databases, followed by finding the antigenicity of PtpA using CLC main workbench tool. The protein-protein interaction network predicts the interface of biological functions of proteins, built by using Cytoscape 2.8.3 version tool for manual literature survey of protein sets. According to the literature the specific interactivity of PtpA with VPS33B of human lead to pathogenesis, and provided a good platform to find the structure of VPS33B as it lacks the 3 dimensional structure in PDB. Homology Modelling of VPS33B provides a significant properties to design a specific drug through screening the drug databases (eDrug3D). The modelled protein has been validated through SAVES server maintained by NIH and UCLA with the standard Ramachandran plot with accuracy of 90.7 %. From our findings the interface residues are very crucial points which has been found through docking the modelled protein and Mycobacterium protein and interface residues were selected manually using PyMol software.
- Źródło:
-
International Letters of Natural Sciences; 2014, 11, 2
2300-9675 - Pojawia się w:
- International Letters of Natural Sciences
- Dostawca treści:
- Biblioteka Nauki
Artykuł