Three-dimensional structure of Plasmodium falciparum knob associated heat shock protein 40 predicted by homology modeling method
Ankita Behl and Prakash Chandra Mishra
Malaria remains one of the world’s widespread diseases and is responsible for enormous worldwide mortality. Increasing emergence of resistant Plasmodium strains impedes the efforts and strategies made to control and eradicate the disease. Cell surface structures termed knobs comprise pathogenesis related protein complexes which facilitate the presentation of major virulence factor ‘PfEMP1’ (Plasmodium falciparum erythrocyte membrane protein 1) on the erythrocyte membrane. A knob associated Hsp40 (heat shock protein 40) ‘PFB0090c’ is implicated in chaperoning knob assembly which underscore its importance in parasite biology. The present study aims to propose a three dimensional structure of PFB0090c. A homology model of complete conserved region including J domain, G/F region and C terminal substrate binding domain was derived based on multiple templates. We show that use of multiple templates increases the quality of the generated model and structure is not biased to a particular template used in homology modeling. The proposed structure of PFB0090c was evaluated for its quality using Verify 3D, Errat and Rampage programs. Since Hsps are considered probable anti-malarial drug targets, our proposed model for PFB0090c may help in structure based drug designing against lethal malaria.
How to cite this article:
Ankita Behl, Prakash Chandra Mishra. Three-dimensional structure of Plasmodium falciparum knob associated heat shock protein 40 predicted by homology modeling method. Pharma Innovation 2018;7(2):202-205.