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Figure 2.
Figure 2. Quantitative comparison of the conformations of the
various MART-1[26/27–35]-based peptides. The Figure shows the
pair-wise superimposition matrix of all conformations of the
peptides, including both molecules in each asymmetric unit for
the structures solved here (MOL 1 and MOL 2), the two
alternative conformations for the ALG nonamer (MOL 1A and MOL
1B), and the ALG and ELA structures of Sliz et al.^24 Values are
RMSD in Å. Superimpositions are via the backbones of
P1−P9 (the first amino acid residue in the decameric peptides
is P0). Values for peptides in the extended conformation (AAG
and ALG) are green; values for peptides in the bulged
conformation (EAA, ELA, and LAG) are blue. Cross-conformational
superimpositions are red. Superimpositions of two molecules in
the asymmetric units of any one structure (i.e. MOL 1 onto MOL
2) are shaded grey. It is of note that the cross-conformational
superimpositions are all close to 2 Å, reflecting the
differences between the bulged and extended conformations.
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