Role of κ→λ light-chain constant-domain switch in the structure and functionality of A17 reactibody

Ponomarenko, N.; Chatziefthimiou, S.D.; Kurkova, I.; Mokrushina, Yu.; Mokrushina, Y.; Stepanova, A.; Smirnov, I.; Avakyan, M.; Bobik, T.; Mamedov, A.; Mitkevich, V.; Belogurov, A.; Fedorova, O.S.; Dubina, M.; Golovin, A.; Lamzin, V.; Friboulet, A.; Makarov, A.A.; Wilmanns, M.; Gabibov, A.

doi:10.1107/S1399004713032446

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 3
(a) 2F_o − F_c electron-density map contoured at the 1.5σ level above the mean (0.4 e Å⁻³) showing the MES molecule, water 147 and the catalytic Tyr-L36. Heavy and light chains are shown in magenta and cyan, respectively. (b) An extended hydrogen-bonding pattern involving the MES molecule and five intact water molecules located close to the A17λ active centre (red dashed lines).

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 3| February 2014| Pages 708-719

doi:10.1107/S1399004713032446

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