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@ARTICLE{Ponomarenko:168905,
      author       = {Ponomarenko, Natalia and Chatziefthymiou, Spyridon and
                      Kurkova, Inna and Mokrushina, Yuliana and Stepanova,
                      Anastasiya and Smirnov, Ivan and Avakyan, Marat and Bobik,
                      Tatyana and Mamedov, Azad and Mitkevich, Vladimir and
                      Belogurov, Alexey and Fedorova, Olga S. and Dubina, Michael
                      and Golovin, Andrey and Lamzin, Victor and Friboulet, Alain
                      and Makarov, Alexander A. and Wilmanns, Matthias and
                      Gabibov, Alexander},
      title        = {{R}ole of κ→λ light-chain constant-domain switch in the
                      structure and functionality of {A}17 reactibody},
      journal      = {Acta crystallographica / D},
      volume       = {70},
      number       = {3},
      issn         = {1399-0047},
      address      = {Copenhagen},
      publisher    = {Munksgaard},
      reportid     = {DESY-2014-02720},
      pages        = {708 - 719},
      year         = {2014},
      abstract     = {The engineering of catalytic function in antibodies
                      requires precise information on their structure. Here,
                      results are presented that show how the antibody domain
                      structure affects its functionality. The previously designed
                      organophosphate-metabolizing reactibody A17 has been
                      re-engineered by replacing its constant κ light chain by
                      the λ chain (A17λ), and the X-ray structure of A17λ has
                      been determined at 1.95 Å resolution. It was found that
                      compared with A17κ the active centre of A17λ is displaced,
                      stabilized and made more rigid owing to interdomain
                      interactions involving the CDR loops from the VL and VH
                      domains. These VL/VH domains also have lower mobility, as
                      deduced from the atomic displacement parameters of the
                      crystal structure. The antibody elbow angle is decreased to
                      126° compared with 138° in A17κ. These structural
                      differences account for the subtle changes in catalytic
                      efficiency and thermodynamic parameters determined with two
                      organophosphate ligands, as well as in the affinity for
                      peptide substrates selected from a combinatorial cyclic
                      peptide library, between the A17κ and A17λ variants. The
                      data presented will be of interest and relevance to
                      researchers dealing with the design of antibodies with
                      tailor-made functions.},
      cin          = {EMBL-User / EMBL},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {PETRA Beamline P14 (POF2-54G14)},
      pid          = {G:(DE-H253)POF2-P14-20130405},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000332406600010},
      pubmed       = {pmid:24598740},
      doi          = {10.1107/S1399004713032446},
      url          = {https://bib-pubdb1.desy.de/record/168905},
}