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. 2021 Mar 9;96(10):e1402–e1412. doi: 10.1212/WNL.0000000000011464

Figure. Structural Analysis of Human BST1 Variants.

Figure

This figure was produced using PyMol software version 2.2.0 and represents the following. (A) Structure of the BST1 dimer bound to ATP-γS (pdb 1ISG). Position of each variant sites is indicated. ATP-γS molecule in the active site is shown as sticks. (B) Close-up view of the p.V85M variant site. Mutated residue is shown in white. Variant would create clashes (red disks) with nearby Ala77 in the core. (C) Close-up view of the p.I101V variant site. Residue is located in the core of the protein, but the variant to a smaller residue results in no clash. (D) Close-up view of the p.V272M variant site. Residues with a prime correspond to chain B. This residue is located at the dimer interface, and the variant would create clashes with the other chain, resulting in a destabilization of the dimer.