Dear Prof.
I have predicted the tertiary structure of wild and mutate MAPT through MUSTER. I can find the difference of structure by visual observation. But I can't discribe the change through terminology. Could you please help me describe the sturcture changes. Thank you very much.
attachment1:wild MAPT
attachment2:G389R MAPT
attachment3:R406W MAPT
Because I don't know the knowldge about protein structure. Could you please forgive my ignorance? I once looked at the description about structure change from wild protein to mutate protein. As follows:
Two significant features of the p.Gly222Arg mutation
could make the membrane transporter dysfunctional.
First, the p.Gly222Arg mutation could disturb the positive
electrostatic potential of the substrate-binding surface by
adding an additional positively charged residue.27,30
Second, the larger side chain could break the rocker switch
of H127 by terminating the helical structure of H1 and
changing the N-Ca dihedral angles (4) of Tyr48 from
68.8 to 92.8 and the Ca-C angles (c) from 24.6 to
84.0 (Figures 4B and 4C). Although the p.Gly255Glu
mutation is not predicted to affect the function of
SLCO2A1, the mutation might alter the structure of the
sixth transmembrane domain as a result of the substitution
of a macromolecular hydrophilic amino acid (Glu)
for a micromolecular hydrophobic amino acid (Gly).
Furthermore, in the protein with the latter mutation,
we found another heterozygous single-base-deletion
(c.1634delA), which would result in a frameshift and a
premature termination codon (p.Asn545Thrfs*15).