Deep molecular modeling and mechanistic insights into type 2A von Willebrand disease with von Willebrand factor A2 domain mutations.

Despite the apparently low extent of changes in local SASAs, their variation falls between 1 and 6 Å [ 2 ], roughly 1 order of magnitude of the minimum amount of SASA variation that identifies buried residues in protein interfaces [ 53 ], indicating a clear trend for cleavage site residues to be more exposed in the mutants than in WT A2.

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