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

Acta Crystallographica Section D: Biological Crystallography

Volumn 70, Issue 3, 2014, Pages 708-719

  Ponomarenko, Natalia ^a   Chatziefthimiou, Spyros D ^b   Kurkova, Inna ^a   Mokrushina, Yuliana ^a   Stepanova, Anastasiya ^a   Smirnov, Ivan ^a   Avakyan, Marat ^a   Bobik, Tatyana ^a   Mamedov, Azad ^a   Mitkevich, Vladimir ^c   Belogurov, Alexey ^a,d   Fedorova, Olga S ^e   Dubina, Michael ^f   Golovin, Andrey ^g   Lamzin, Victor ^b   Friboulet, Alain ^h   Makarov, Alexander A ^c   Wilmanns, Matthias ^b   Gabibov, Alexander ^a,d,g  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^d INSTITUTE OF GENE BIOLOGY   (Russian Federation)

^e INSTITUTE OF CHEMICAL BIOLOGY AND FUNDAMENTAL MEDICINE   (Russian Federation)

^f ST PETERSBURG ACADEMIC UNIVERSITY   (Russian Federation)

^g MOSCOW STATE UNIVERSITY   (Russian Federation)

^h UNIVERSITÉ DE TECHNOLOGIE DE COMPIÈGNE   (France)

Author keywords

A17 reactibody; Antibodies

Indexed keywords

ANTIBODY; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN KAPPA CHAIN; IMMUNOGLOBULIN LAMBDA CHAIN; RECOMBINANT PROTEIN;

A17 REACTIBODY; ARTICLE; CHEMISTRY; COMPARATIVE STUDY; COMPLEMENTARITY DETERMINING REGION; CRYSTALLIZATION; GENETICS; HUMAN; IMMUNOGLOBULIN CONSTANT REGION; IMMUNOGLOBULIN GENE; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

A17 REACTIBODY; ANTIBODIES;

COMPLEMENTARITY DETERMINING REGIONS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; HUMANS; IMMUNOGLOBULIN CONSTANT REGIONS; IMMUNOGLOBULIN HEAVY CHAINS; IMMUNOGLOBULIN KAPPA-CHAINS; IMMUNOGLOBULIN LAMBDA-CHAINS; IMMUNOGLOBULIN SWITCH REGION; RECOMBINANT PROTEINS; THERMODYNAMICS;

EID: 84896787281     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S1399004713032446     Document Type: Article

References (51)

1. Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H. & Adams, P. D. (2012). Acta Cryst. D68, 352-367.
2. Eddleston, M., Buckley, N. A., Eyer, P. & Dawson, A. H. (2008). Lancet, 371, 597-607.
3. Ekiert, D. C. et al. (2012). Nature (London), 489, 526-532.
4. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
5. Evans, P. (2006). Acta Cryst. D62, 72-82.
6. Gabibov, A. G. et al. (2011). FASEB J. 25, 4211-4221.
7. Golinelli-Pimpaneau, B., Goncalves, O., Dintinger, T., Blanchard, D., Knossow, M. & Tellier, C. (2000). Proc. Natl Acad. Sci. USA, 97, 9892-9895.
8. Guddat, L. W., Shan, L., Anchin, J. M., Linthicum, D. S. & Edmundson, A. B. (1994). J. Mol. Biol. 236, 247-274.
9. Guddat, L. W., Shan, L., Fan, Z.-C., Andersen, K. N., Rosauer, R., Linthicum, D. S. & Edmundson, A. B. (1995). FASEB J. 9, 101-106.
10. Guenaga, J. & Wyatt, R. T. (2012). PLoS Pathog. 8, e1002806.
11. Heine, A., Stura, E. A., Yli-Kauhaluoma, J. T., Gao, C., Deng, Q., Beno, B. R., Houk, K. N., Janda, K. D. & Wilson, I. A. (1998). Science, 279, 1934-1940.
12. Huber, R., Deisenhofer, J., Colman, P. M., Matsushima, M. & Palm, W. (1976). Nature (London), 264, 415-420.
13. Jiang, X., Burke, V., Totrov, M., Williams, C., Cardozo, T., Gorny, M. K., Zolla-Pazner, S. & Kong, X.-P. (2010). Nature Struct. Mol. Biol. 17, 955-961.
14. Kabsch, W. (2010). Acta Cryst. D66, 133-144.
15. Kabsch, W., Kabsch, H. & Eisenberg, D. (1976). J. Mol. Biol. 100, 283-291.
16. Kaneko, E. & Niwa, R. (2011). BioDrugs, 25, 1-11.
17. Karplus, P. A. & Diederichs, K. (2012). Science, 336, 1030-1033.
18. Klohn, P. C., Wuellner, U., Zizlsperger, N., Zhou, Y., Tavares, D., Berger, S., Zettlitz, K. A., Proetzel, G., Yong, M., Begent, R. H. & Reichert, J. M. (2013). MAbs, 5, 178-201.
19. Koivunen, E., Wang, B. & Ruoslahti, E. (1994). J. Cell Biol. 124, 373-380.
20. Krissinel, E. & Henrick, K. (2004). Acta Cryst. D60, 2256-2268.
21. Krissinel, E. & Henrick, K. (2007). J. Mol. Biol. 372, 774-797.
22. Kuzmic, P. (1996). Anal. Biochem. 237, 260-273.
23. Landolfi, N. F., Thakur, A. B., Fu, H., Vá squez, M., Queen, C. & Tsurushita, N. (2001). J. Immunol. 166, 1748-1754.
24. Langer, G. G., Cohen, S. X., Perrakis, A. & Lamzin, V. S. (2008). Nature Protoc. 3, 1171-1179.
25. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). J. Appl. Cryst. 26, 283-291.
26. Lindorff-Larsen, K., Piana, S., Palmo, K., Maragakis, P., Klepeis, J. L., Dror, R. O. & Shaw, D. E. (2010). Proteins, 78, 1950-1958.
27. Lingwood, D., McTamney, P. M., Yassine, H. M., Whittle, J. R. R., Guo, X., Boyington, J. C., Wei, C.-J. & Nabel, G. J. (2012). Nature (London), 489, 566-570.
28. Long, F., Vagin, A. A., Young, P. & Murshudov, G. N. (2008). Acta Cryst. D64, 125-132.
29. Lu, Z.-J., Deng, S.-J., Huang, D.-G., He, Y., Lei, M., Zhou, L. & Jin, P. (2012). World J. Biol. Chem. 3, 187-196.
30. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C. & Read, R. J. (2007). J. Appl. Cryst. 40, 658-674.
31. Mitkevich, V. A., Schulga, A. A., Ermolyuk, Y. S., Lobachov, V. M., Chekhov, V. O., Yakovlev, G. I., Hartley, R. W., Pace, C. N., Kirpichnikov, M. P. & Makarov, A. A. (2003). Biophys. Chem. 105, 383-390.
32. Murshudov, G. N., Skubá k, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F. & Vagin, A. A. (2011). Acta Cryst. D67, 355-367.
33. Narciso, J. E. T., Uy, I. D. C., Cabang, A. B., Chavez, J. F. C., Pablo, J. L. B., Padilla-Concepcion, G. P. & Padlan, E. A. (2011). New Biotechnol. 28, 435-447.
34. Narciso, J. E. T., Uy, I. D. C., Cabang, A. B., Chavez, J. F. C., Pablo, J. L. B., Padilla-Concepcion, G. P. & Padlan, E. A. (2012). Philipp. Sci. Lett. 5, 63-89.
35. Padlan, E. A. (1994). Mol. Immunol. 31, 169-217.
36. Parmley, S. F. & Smith, G. P. (1988). Gene, 73, 305-318.
37. Ponomarenko, N. A., Pillet, D., Paon, M., Vorobiev, I. I., Smirnov, I. V., Adenier, H., Avalle, B., Kolesnikov, A. V., Kozyr, A. V., Thomas, D., Gabibov, A. G. & Friboulet, A. (2007). Biochemistry, 46, 14598-14609.
38. Privett, H. K., Kiss, G., Lee, T. M., Blomberg, R., Chica, R. A., Thomas, L. M., Hilvert, D., Houk, K. N. & Mayo, S. L. (2012). Proc. Natl Acad. Sci. USA, 109, 3790-3795.
39. Pronk, S., Pá ll, S., Schulz, R., Larsson, P., Bjelkmar, P., Apostolov, R., Shirts, M. R., Smith, J. C., Kasson, P. M., van der Spoel, D., Hess, B. & Lindahl, E. (2013). Bioinformatics, 29, 845-854.
40. Reshetnyak, A. V., Armentano, M. F., Ponomarenko, N. A., Vizzuso, D., Durova, O. M., Ziganshin, R., Serebryakova, M., Govorun, V., Gololobov, G., Morse, H. C. III, Friboulet, A., Makker, S. P., Gabibov, A. G. & Tramontano, A. (2007). J. Am. Chem. Soc. 129, 16175-16182.
41. Sapparapu, G., Planque, S., Mitsuda, Y., McLean, G., Nishiyama, Y. & Paul, S. (2012). J. Biol. Chem. 287, 36096-36104.
42. Smirnov, I. et al. (2011). Proc. Natl Acad. Sci. USA, 108, 15954-15959.
43. Sotriffer, C. A., Rode, B. M., Varga, J. M. & Liedl, K. R. (2000). Biophys. J. 79, 614-628.
44. Stanfield, R. L., Gorny,M. K., Zolla-Pazner, S. &Wilson, I. A. (2006). J. Virol. 80, 6093-6105.
45. Stanfield, R. L., Zemla, A., Wilson, I. A. & Rupp, B. (2006). J. Mol. Biol. 357, 1566-1574.
46. Turner, J. M., Larsen, N. A., Basran, A., Barbas, C. F. III, Bruce, N. C., Wilson, I. A. & Lerner, R. A. (2002). Biochemistry, 41, 12297-12307.
47. Vagin, A. & Teplyakov, A. (2010). Acta Cryst. D66, 22-25.
48. Vincent, K. J. & Zurini, M. (2012). Biotechnol. J. 7, 1444-1450.
49. Yribarren, A. S., Thomas, D., Friboulet, A. & Avalle, B. (2003). Eur. J. Biochem. 270, 2789-2795.
50. Zakharov, A. V., Smirnov, I. V., Serebryakova, M. V., Dronina, M. A., Kaznacheeva, A. V., Kurkova, I. N., Belogurov, A. A., Friboulet, A., Ponomarenko, N. A., Gabibov, A. G. & Bobik, T. V. (2011). Mol. Biol. 45, 74-81.
51. Zheng, L., Goddard, J. P., Baumann, U. & Reymond, J. L. (2004). J. Mol. Biol. 341, 807-814.