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 3
Structure FabXol1² of the omalizumab-derived Leu158Pro mutant (FabXol1). (a) In FabXol1^2C (pink), residues Pro158–Ser160 form an interface with the Cκ domain from FabXol1^2A (gray) and the V_H domain from FabXol1^2B (yellow). (b) The FabXol1^2A (gray) and FabXol1^2B (green) CDRs adopt similar conformations, and both contact the V_L and Cκ domains from a symmetry-related molecule. A shift in the position of the symmetry-related molecule relative to FabXol1^2A reduces the interface area, and only a single hydrogen bond is formed between Tyr102 (CDRH3) and Asp174 (Cκ domain). (c) Binding of a glycerol molecule (GOL) in FabXol1^2C (gray) causes the Tyr33 and His101 side chains to adopt substantially different positions compared with those in FabXol1 (pink). (d) In FabXol1^2C (gray), Thr30 and Ser31 form hydrogen bonds with Thr73 and Ser28, respectively, from a symmetry-related molecule (blue). Tyr102 packs against Gly15 and Gly16 from a different symmetry-related molecule (yellow).

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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