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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">dan</journal-id><journal-title-group><journal-title xml:lang="ru">Доклады Национальной академии наук Беларуси</journal-title><trans-title-group xml:lang="en"><trans-title>Doklady of the National Academy of Sciences of Belarus</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">1561-8323</issn><issn pub-type="epub">2524-2431</issn><publisher><publisher-name>The Republican Unitary Enterprise Publishing House "Belaruskaya Navuka"</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.29235/1561-8323-2020-64-2-193-198</article-id><article-id custom-type="elpub" pub-id-type="custom">dan-870</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>БИОЛОГИЯ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>BIOLOGY</subject></subj-group></article-categories><title-group><article-title>Молекулярные механизмы высокоаффинного взаимодействия белка tBid с митохондриальным комплексом МТСН2-МОАР-1</article-title><trans-title-group xml:lang="en"><trans-title>Molecular mechanisms of high-affinity interaction of the protein tBid with the mitochondrial complex МТСН2-МОАР-1</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Дудко</surname><given-names>А. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Dudko</surname><given-names>H. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Дудко Анна Викторовна – мл. науч. сотрудник.</p><p>ул. Академическая, 27, 220072, Минск</p></bio><bio xml:lang="en"><p>Dudko Hanna V. – Junior researcher.</p><p>27, Akademicheskaya Str., 220072, Minsk</p></bio><email xlink:type="simple">dudko@ibp.org.by</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Урбан</surname><given-names>В. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Urban</surname><given-names>V. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Урбан Виктор Андреевич – мл. науч. сотрудник.</p><p>ул. Академическая, 27, 220072, Минск</p></bio><bio xml:lang="en"><p>Urban Viktar A. – Junior researcher.</p><p>27, Akademicheskaya Str., 220072, Minsk</p></bio><email xlink:type="simple">urban@ibp.org.by</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Вересов</surname><given-names>В. Г.</given-names></name><name name-style="western" xml:lang="en"><surname>Veresov</surname><given-names>V. G.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Вересов Валерий Гавриилович – д-р биол. наук, гл. науч. сотрудник.</p><p>ул. Академическая, 27, 220072, Минск</p></bio><bio xml:lang="en"><p>Veresov Valery G. – D. Sc. (Biology), Chief researcher.</p><p>27, Akademicheskaya Str., 220072, Minsk</p></bio><email xlink:type="simple">veresov@ibp.org.by</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Институт биофизики и клеточной инженерии Национальной академии наук Беларуси</institution></aff><aff xml:lang="en"><institution>Institute of Biophysics and Cell Engineering of the National Academy of Sciences of Belarus</institution></aff></aff-alternatives><pub-date pub-type="collection"><year>2020</year></pub-date><pub-date pub-type="epub"><day>17</day><month>05</month><year>2020</year></pub-date><volume>64</volume><issue>2</issue><fpage>193</fpage><lpage>198</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Дудко А.В., Урбан В.А., Вересов В.Г., 2020</copyright-statement><copyright-year>2020</copyright-year><copyright-holder xml:lang="ru">Дудко А.В., Урбан В.А., Вересов В.Г.</copyright-holder><copyright-holder xml:lang="en">Dudko H.V., Urban V.A., Veresov V.G.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://doklady.belnauka.by/jour/article/view/870">https://doklady.belnauka.by/jour/article/view/870</self-uri><abstract><p>Митохондриальный белок MTCH2 (mitochondrial carrier homolog 2) играет важную роль в осуществлении апоптоза, являясь рецептором для про-апоптотического белка tBid на наружной мембране митохондрий (НММ). Ранее было установлено, что белок MOAP-1 (modulator of apoptosis-1) необходим для эффективного связывания белка tBid с его рецептором на НММ, однако структурные детерминанты этой регуляции остаются неясными. В данном сообщении представлены результаты установления структурных факторов действия белка MOAP-1, обусловливающих эффективное связывание белка tBid с рецептор-подобным белком MTCH2</p></abstract><trans-abstract xml:lang="en"><p>Mitochondrial carrier homolog 2 (MTCH2) is a protein that plays an important role in the execution of apoptosis being a receptor for tBid in the outer membrane of mitochondria. Previously, it has been shown that the binding of the modulator of apoptosis-1 (MOAP-1) protein to MTCH2 is required for the efficient MTCH2-mediated recruitment of tBid to mitochondria and, in contrast, tBid is required for the MOAP-1 recruitment to mitochondria, but the structure understanding of these phenomena is absent. In this study, we have provided structural insights into the mechanisms of regulation of the MTCH2 receptor function for tBid by MOAP-1.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>апоптоз</kwd><kwd>MTCH2</kwd><kwd>tBid</kwd><kwd>MOAP-1</kwd><kwd>Bax</kwd><kwd>Bak</kwd></kwd-group><kwd-group xml:lang="en"><kwd>apoptosis</kwd><kwd>MTCH2</kwd><kwd>tBid</kwd><kwd>MOAP-1</kwd><kwd>Bax</kwd><kwd>Bak</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy / P. E. Czabotar [et al.] // Nat. Rev. Mol. Cell Biol. – 2014. – Vol. 15, N 1. – P. 49–63. https://doi.org/10.1038/nrm3722</mixed-citation><mixed-citation xml:lang="en">Czabotar P. E., Lessene G., Strasser A., Adams J. M. Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy. Nature Reviews Molecular Cell Biology, 2014, vol. 15, no. 1, pp. 49–63. https://doi.org/10.1038/nrm3722</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Martinou, J. C. Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics / J. C. Martinou, R. J. Youle // Dev. Cell. – 2011. – Vol. 21, N 1. – P. 92–101. https://doi.org/10.1016/j.devcel.2011.06.017</mixed-citation><mixed-citation xml:lang="en">Martinou J. C., Youle R. J. Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics. Developmental Cell, 2011, vol. 21, no. 1, pp. 92–101. https://doi.org/10.1016/j.devcel.2011.06.017</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">MOAP-1 Mediates Fas-Induced Apoptosis in Liver by Facilitating tBid Recruitment to Mitochondria / C. Tan [et al]. // Cell Rep. – 2016. – Vol. 16, N 1. – P. 174–185. https://doi.org/10.1016/j.celrep.2016.05.068</mixed-citation><mixed-citation xml:lang="en">Tan C. T., Zhou Q.-L., Su Y.-C., Fu N. Y., Chang H.-C., Tao R. N., Sukumaran S. K., Baksh S., Tan Y.-J., Sabapathy K., Yu C.-D., Yu V. C. MOAP-1 Mediates Fas-Induced Apoptosis in Liver by Facilitating tBid Recruitment to Mitochondria. Cell Reports, 2016, vol. 16, no. 1, pp. 174–185. https://doi.org/10.1016/j.celrep.2016.05.068</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Veresov, V. G. Structural insights into proapoptotic signaling mediated by MTCH2, VDAC2, TOM40 and TOM22 / V. G. Veresov, A. I. Davidovskii // Cellular Signalling. – 2014. – Vol. 26, N 2. – P. 370–382. https://doi.org/10.1016/j.cellsig.2013.11.016</mixed-citation><mixed-citation xml:lang="en">Veresov V. G., Davidovskii A. I. Structural insights into proapoptotic signaling mediated by MTCH2, VDAC2, TOM40 and TOM22. Cellular Signalling, 2014, vol. 26, no. 2, pp. 370–382. https://doi.org/10.1016/j.cellsig.2013.11.016</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">BID is cleaved by caspase-8 within a native complex on the mitochondrial membrane / Z. T. Schug [el al.] // Cell Death Differ. – 2011. – Vol. 18, N 3. – P. 538–548. https://doi.org/10.1038/cdd.2010.135</mixed-citation><mixed-citation xml:lang="en">Schug Z. T., Gonzalvez F., Houtkooper R. H., Vaz F. M., Gottlieb E. BID is cleaved by caspase-8 within a native complex on the mitochondrial membrane. Cell Death &amp; Differentiation, 2011, vol. 18, no. 3, pp. 538–548. https://doi.org/10.1038/cdd.2010.135</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Roy, A. I-TASSER: a unified platform for automated protein structure and function prediction / A. Roy, A. Kucukural, Y. Zhang // Nat. Protocols. – 2010. – Vol. 5, N 3. – P. 725–738. https://doi.org/10.1038/nprot.2010.5</mixed-citation><mixed-citation xml:lang="en">Roy A., Kucukural A., Zhang Y. I-TASSER: a unified platform for automated protein structure and function prediction. Nature Protocols, 2010, vol. 5, no. 3, pp. 725–738. https://doi.org/10.1038/nprot.2010.5</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Heo, L. GalaxyRefine: Protein structure refinement driven by side-chain repacking / L. Heo, H. Park, C. Seok // Nucleic Acids Research. – 2013. – Vol. 41, N W1. – P. W384–W388. https://doi.org/10.1093/nar/gkt458</mixed-citation><mixed-citation xml:lang="en">Heo L., Park H., Seok C. GalaxyRefine: Protein structure refinement driven by side-chain repacking. Nucleic Acids Research, 2013, vol. 41, no. W1, pp. W384–W388. https://doi.org/10.1093/nar/gkt458</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">OPM: orientations of proteins in membranes database / M. A. Lomize [et al.] // Bioinformatics. – 2006. – Vol. 22, N 5. – P. 623–625. https://doi.org/10.1093/bioinformatics/btk023</mixed-citation><mixed-citation xml:lang="en">Lomize M. A., Lomize A. L., Pogozheva I. D., Mosberg H. I. OPM: orientations of proteins in membranes database. Bioinformatics, 2006, vol. 22, no. 5, pp. 623–625. https://doi.org/10.1093/bioinformatics/btk023</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">PIPER: an FFT-Based protein docking program with pairwise potentials / D. Kozakov [et al.] // Proteins. – 2006. – Vol. 65, N 2. – P. 392–406. https://doi.org/10.1002/prot.21117</mixed-citation><mixed-citation xml:lang="en">Kozakov D., Brenke R., Comeau S. R., Vajda S. PIPER: an FFT-Based protein docking program with pairwise potentials. Proteins: Structure, Function, and Bioinformatics, 2006, vol. 65, no. 2, pp. 392–406. https://doi.org/10.1002/prot.21117</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Heo, L. GalaxyRefineComplex: Refinement of protein-protein complex model structures driven by interface repacking / L. Heo, H. Lee, C. Seok // Sci. Rep. – 2016. – Vol. 6, N 1. – P. 32153. https://doi.org/10.1038/srep32153</mixed-citation><mixed-citation xml:lang="en">Heo L., Lee H., Seok C. GalaxyRefineComplex: Refinement of protein-protein complex model structures driven by interface repacking. Scientific Reports, 2016, vol. 6, no. 1, pp. 32153. https://doi.org/10.1038/srep32153</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Mandell, D. J. Sub-angstrom accuracy in protein loop reconstruction by robotics-inspired conformational sampling / D. J. Mandell, E. A. Coutsias, T. Kortemme // Nature Methods. – 2009. – Vol. 6, N 8. – P. 551–552. https://doi.org/10.1038/nmeth0809-551</mixed-citation><mixed-citation xml:lang="en">Mandell D. J., Coutsias E. A., Kortemme T. Sub-angstrom accuracy in protein loop reconstruction by robotics-inspired conformational sampling. Nature Methods, 2009, vol. 6, no. 8, pp. 551–552. https://doi.org/10.1038/nmeth0809-551</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations / J. J. Gray [et al.] // J. Molecular Biol. – 2003. – Vol. 331, N 1. – P. 281–299. https://doi.org/10.1016/s0022-2836(03)00670-3</mixed-citation><mixed-citation xml:lang="en">Gray J. J., Moughon S., Wang C., Schueler-Furman O., Kuhlman B., Rohl C. A., Baker D. Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations. Journal of Molecular Biology, 2003, vol. 331, no. 1, pp. 281–299. https://doi.org/10.1016/s0022-2836(03)00670-3</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">PRODIGY: a web server for predicting the binding affinity of protein-protein complexes / L. C. Xue [et al.] // Bioinformatics. – 2016. – Vol. 32, N 23. – P. 3676–3678. https://doi.org/10.1093/bioinformatics/btw514</mixed-citation><mixed-citation xml:lang="en">Xue L. C., Rodrigues J. P., Kastritis P. L., Bonvin A. M., Vangone A. PRODIGY: a web server for predicting the binding affinity of protein-protein complexes. Bioinformatics, 2016, vol. 32, no. 23, pp. 3676–3678. https://doi.org/10.1093/bioinformatics/btw514</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Protocols for Molecular Modeling with Rosetta3 and RosettaScripts / B. J. Bender [et al.] // Biochemistry. – 2016. – Vol. 55, N 34. – P. 4748–4763. https://doi.org/10.1021/acs.biochem.6b00444</mixed-citation><mixed-citation xml:lang="en">Bender B. J., Cisneros A., Duran A. M., Finn J. A., Fu D., Lokits A. D., Mueller B. K., Sangha A. K., Sauer M. F., Sevy A. M., Sliwoski G., Sheehan J. H., DiMaio F., Meiler J., Moretti R. Protocols for Molecular Modeling with Rosetta3 and RosettaScripts. Biochemistry, 2016, vol. 55, no. 34, pp. 4748–4763. https://doi.org/10.1021/acs.biochem.6b00444</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Sukhwal, A. PPCheck: A Webserver for the Quantitative Analysis of Protein-Protein Interfaces and Prediction of Residue Hotspots / A. Sukhwal, R. Sowdhamini // Bioinformatics and Biology Insights. – 2015. – Vol. 9. – P. 141–151. https://doi.org/10.4137/bbi.s25928</mixed-citation><mixed-citation xml:lang="en">Sukhwal A., Sowdhamini R. PPCheck: A Webserver for the Quantitative Analysis of Protein-Protein Interfaces and Prediction of Residue Hotspots. Bioinformatics and Biology Insights, 2015, vol. 9, pp. 141–151. https://doi.org/10.4137/bbi.s25928</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
