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Fig. 6 | BMC Structural Biology

Fig. 6

From: Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins

Fig. 6

Flexibility and contact network analysis. a. DynaMine prediction of F57A flexibility. b. DynaMine prediction of flexibility of the CMT disease mutations in P2. Our residue numbering differs by − 1 from the mutation reports, to comply with the conventional numbering of residues in P2 and other FABP structures. c. Mapping of central residues onto the P2 structure. The structure shown is the liganded structure of the P38G mutant during MD simulations, to highlight the opening. The centralities were calculated from the unliganded crystal structures. The bound fatty acid is shown as a magenta surface and Phe57 in orange. Residues having high Z scores of centrality are indicated in blue, and the ones showing higher centrality in F57A than the wild-type P2 in yellow. Note how the opening β flap has no residues of high centrality (red circle). See Additional file 1: Figure S1 for more details

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