Pvs25 is a protein of unique 3D structure, and it is characterized by the presence of repeated EGF-like domains and 11 disulfide bonds. It is a very important candidate for the transmission-blocking malaria vaccine, as it plays an important role in mosquito infection by Plasmodium parasites. Recently, the X-ray structure of the protein complexed with the transmission blocking antibody 2A8 has been reported. In this study, we report the loop reorganization of the Pvs25 protein based on configurational entropy calculations and dihedral principal component analysis as revealed from the protein complex and free molecular dynamics simulations. While the total entropy of the protein was estimated to be almost the same in the free and complex trajectories, the partition of the entropy contribution in the loop fragments of the protein revealed interesting entropy reallocation after the 2A8 antibody binding. Interestingly, the 51-71 protein loop experienced a significant reduction in its configurational entropy, while other parts of the protein did not show any difference in it, or even showed an entropy increase. This trend in entropy redistribution was found to be in direct relationship with specific interactions with the antibody's binding site. Results from root-mean-square fluctuations/deviations and dihedral angle principal component analysis further support this finding.