Engineering the Fab fragment of the anti-IgE omalizumab to prevent Fab crystallization and permit IgE-Fc complex crystallization

Mitropoulou, A.N.; Ceska, T.; Heads, J.T.; Beavil, A.J.; Henry, A.J.; McDonnell, J.M.; Sutton, B.J.; Davies, A.M.

doi:10.1107/S2053230X20001466

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 4
Structure of the omalizumab-derived Ser81Arg, Gln83Arg, Leu158Pro mutant (FabXol3). (a) In the FabXol3 (gray) and FabXol2 (pink) structures, Arg81 forms hydrogen bonds with Asn156. In the FabXol3 structure, Arg81 contacts Pro158, while Leu158 is partially disordered in the FabXol2 structure. Arg83 does not form any crystal packing interactions. (b) In the FabXol3 structure, CDRH1 and CDRH3 residues (gray) contact the V_L domain of a symmetry-related molecule (green). Hydrogen bonds are depicted by black lines. (c) Asp55 (CDRH2) forms a salt bridge with Lys211 from the Cκ domain of a symmetry-related molecule (blue).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 76| Part 3| March 2020| Pages 116-129

https://doi.org/10.1107/S2053230X20001466

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