Crystal structure of N-terminally hexahistidine-tagged Onchocerca volvulus macrophage migration inhibitory factor-1

Kimble, A.D.; Dawson, O.C.O.; Liu, L.; Subramanian, S.; Cooper, A.; Battaile, K.; Craig, J.; Harmon, E.; Myler, P.; Lovell, S.; Asojo, O.A.

doi:10.1107/S2053230X24010550

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Comparison of tautomerase inhibitor-binding cavities in surface plots of hMIF-1 (cyan; PDB entry 1mif), AceMIF (purple; PDB entry 3rf4) and His-OvMIF-1 (gray). Furosemide (shown as sticks), a selective inhibitor of AceMIF, fits best into its larger cavity of AceMIF, hMIF has a smaller cavity and His-OvMIF-1 lacks the cavity (top row). The superposed trimer surfaces are shown in the bottom row. The structure of His-OvMIF-1 with the N-terminal tag in magenta is shown, as is the structure of OvMIF-1 generated by deleting the tag. OvMIF-1 has a more open cavity than the other structures.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 80| Part 12| December 2024|

https://doi.org/10.1107/S2053230X24010550

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