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 5
(a) Superposition of the A17λ and A17κ variable domains. A17λ CDR loops are shown in magenta and A17κ CDR loops are shown in blue. The flip of the Trp-L92 side chain is indicated. (b) The flipping of Trp-L92 provides the enlargement of the hydrophobic pocket surface (Trp-L92–Phe-L100) and the formation of a kind of lid above the cavity entrance. The light chain of A17κ is shown in cyan and the heavy chain is shown in brown; the light chain of A17λ is shown in green and the heavy chain in shown in magenta.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

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

doi:10.1107/S1399004713032446

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