 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](kw5080fig3mag.jpg)
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Figure 3
Superposition of the region surrounding the Gly89–Val90 peptide bond from the two crystal forms of FKBP12.6 and comparison with the corresponding segment of the first FKBP domain of FKBP51. The C atoms of the P21 crystal form structure of cysteine-free FKBP12.6 are colored green, while those of the P3121 crystal form structure are shown in yellow (a). The peptide linkage between Gly89 and Val90 is flipped in the P21 crystal form compared with the P3121 crystal form as well as in comparison to either the rapamycin-inhibited FKBP12.6 structure (Deivanayagam et al., 2000  ) or the high-resolution apo FKBP12 structure (Szep et al., 2009). In (b), this segment of the P21 crystal form structure of cysteine-free FKBP12.6 is superimposed upon the homologous segment from the 1.00 Å resolution structure of the first FKBP domain of FKBP51 (PDB entry 3o5p
; Bracher et al., 2011), which is illustrated in blue. |
![[Figure 3]](kw5080fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
