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@ARTICLE{Dubovskii:478829,
      author       = {Dubovskii, Peter V. and Dubova, Kira M. and Bourenkov, Gleb
                      and Starkov, Vladislav G. and Konshina, Anastasia G. and
                      Efremov, Roman G. and Utkin, Yuri N. and Samygina, Valeriya
                      R.},
      title        = {{V}ariability in the {S}patial {S}tructure of the {C}entral
                      {L}oop in {C}obra {C}ytotoxins {R}evealed by {X}-ray
                      {A}nalysis and {M}olecular {M}odeling},
      journal      = {Toxins},
      volume       = {14},
      number       = {2},
      issn         = {2072-6651},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {PUBDB-2022-02779},
      pages        = {149},
      year         = {2022},
      abstract     = {Cobra cytotoxins (CTs) belong to the three-fingered protein
                      family and possess membrane activity. Here, we studied
                      cytotoxin 13 from Naja naja cobra venom (CT13Nn). For the
                      first time, a spatial model of CT13Nn with both “water”
                      and “membrane” conformations of the central loop
                      (loop-2) were determined by X-ray crystallography. The
                      “water” conformation of the loop was frequently
                      observed. It was similar to the structure of loop-2 of
                      numerous CTs, determined by either NMR spectroscopy in
                      aqueous solution, or the X-ray method. The “membrane”
                      conformation is rare one and, to date has only been observed
                      by NMR for a single cytotoxin 1 from N. oxiana (CT1No) in
                      detergent micelle. Both CT13Nn and CT1No are S-type CTs.
                      Membrane-binding of these CTs probably involves an
                      additional step—the conformational transformation of the
                      loop-2. To confirm this suggestion, we conducted molecular
                      dynamics simulations of both CT1No and CT13Nn in the Highly
                      Mimetic Membrane Model of
                      palmitoiloleoylphosphatidylglycerol, starting with their
                      “water” NMR models. We found that the both toxins
                      transform their “water” conformation of loop-2 into the
                      “membrane” one during the insertion process. This
                      supports the hypothesis that the S-type CTs, unlike their
                      P-type counterparts, require conformational adaptation of
                      loop-2 during interaction with lipid membranes.},
      cin          = {EMBL-User / EMBL},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35202176},
      UT           = {WOS:000762016100001},
      doi          = {10.3390/toxins14020149},
      url          = {https://bib-pubdb1.desy.de/record/478829},
}