 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 4]](va5039fig4mag.jpg)
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Figure 4
Structural differences between FLL27D and FLWT are limited to the dimerization-interface region. (a) Superimposition of FLL27D (gray) and FLWT (green). Crystallographic models of the ligands are shown in cartoon representation with indication of the twofold-symmetry axis (inset) or as ribbon diagrams (main panel); the side chain of Asp27 in FLL27D is shown as sticks and FLT3 is shown in surface representation. With the exception of the αB–βA loop, the main chain of both FLL27D molecules superimposes very well (average Cα r.m.s.d. of 0.85 Å) with the main chain of all four FLWT copies (PDB entry 1ete). (b) The asymmetric unit of FLL27D crystals features a top-to-top packing of molecules. This topology is distinct from the twofold-symmetry axis within one FLWT molecule and supports the L27D mutation preventing dimerization even in the context of crystal packing. (c) Detail of the superimposed αB–βA loop of FLL27D (gray) and FLWT (green). Loop residues are shown as sticks. Hydrogen bonds are indicated by dashed lines. (d) Detail of the superimposed αB–βA loops of FLL27D and FLWT, as viewed from the second FLWT protomer. FLWT is colored according the Eisenberg hydrophobicity scale (red is more hydrophobic); key residues of FLL27D are shown as sticks. Hydrogen bonds are indicated by dashed lines. |
![[Figure 4]](va5039fig4.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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