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. 2021 Mar 10;7:620554. doi: 10.3389/fmolb.2020.620554

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Copyright © 2021 Prabantu, Naveenkumar and Srinivasan.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The PSN of human serum albumin protein at the site of mutation and function in the wildtype (PDB ID: 1N5U) and mutant (PDB ID: 1HK3) is shown. The node corresponding to the mutation site makes an edge with a hub node L238 (green sphere) in (A) the wildtype PSN which is lost in the case of (B) the mutant PSN. It is observed that hubs near to the binding site (K240) are lost, which is indicative of the increase in proximity between the nodes. It has been reported that the mutant structure is able to better accommodate a substrate with greater binding affinity which leads to the FDH disease condintion. Hubs unique to the wildtype and mutant are show in green and cyan sphere representation respectively, those hubs that are retained are shown in red.