Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 68, Issue 11, 2012, Pages 1289-1293

  García Fernández, Rossana ^a   Pons, Tirso ^b   Meyer, Arne ^c   Perbandt, Markus ^d,e   González González, Yamile ^a   Gil, Dayrom ^a   De Los Angeles Chávez, María ^a   Betzel, Christian ^d   Redecke, Lars ^d  

^a UNIVERSITY OF HAVANA   (Cuba)

^b Structural Biology and Biocomputing Programme   (Spain)

^c Xtal Concepts   (Germany)

^d UNIVERSITY OF HAMBURG   (Germany)

^e UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF   (Germany)

Author keywords

BPTI Kunitz type domains; protease inhibitors

Indexed keywords

RECOMBINANT PROTEIN; SHPI PROTEINASE INHIBITOR; SOYBEAN TRYPSIN INHIBITOR;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; HYDROGEN BOND; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEA ANEMONE; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEA ANEMONES; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN; TRYPSIN INHIBITOR, KUNITZ SOYBEAN;

INVERTEBRATA; MAMMALIA; STICHODACTYLA HELIANTHUS;

EID: 84869058334     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309112039085     Document Type: Article

References (30)

1. Antuch, W., Berndt, K. D., Chá vez, M. A., Delfi'n, J. & Wüthrich, K. (1993). Eur. J. Biochem. 212, 675-684.
2. Betzel, C., Dauter, Z., Genov, N., Lamzin, V., Navaza, J., Schnebli, H. P., Visanji, M. & Wilson, K. S. (1993). FEBS Lett. 317, 185-188.
3. Burgering, M. J., Orbons, L. P., van der Doelen, A., Mulders, J., Theunissen, H. J., Grootenhuis, P. D., Bode,W., Huber, R. & Stubbs,M. T. (1997). J. Mol. Biol. 269, 395-407.
4. Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S. & Richardson, D. C. (2010). Acta Cryst. D66, 12-21.
5. Cromwell, M. E. M., Hilario, E. & Jacobson, F. (2006). AAPS J. 8, E572-E579.
6. Czapinska, H., Otlewski, J., Krzywda, S., Sheldrick, G. M. & Jaskó lski, M. (2000). J. Mol. Biol. 295, 1237-1249.
7. Deisenhofer, J. & Steigemann, W. (1975). Acta Cryst. B31, 238-250.
8. Delfi'n, J., Marti'nez, I., Antuch, W., Morera, V., Gonzá lez, Y., Rodri'guez, R., Ma'rquez, M., Saroyá n, A., Larionova, N., Di'az, J., Padró n, G. & Chá vez, M. (1996). Toxicon, 34, 1367-1376.
9. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. (2010). Acta Cryst. D66, 486-501.
10. Erlanger, B. F., Kokowsky, N. & Cohen, W. (1961). Arch. Biochem. Biophys. 95, 271-278.
11. Finn, R. D., Mistry, J., Tate, J., Coggill, P., Heger, A., Pollington, J. E., Gavin, O. L., Gunasekaran, P., Ceric, G., Forslund, K., Holm, L., Sonnhammer, E. L., Eddy, S. R. & Bateman, A. (2010). Nucleic Acids Res. 38, D211- D222.
12. Fischer, H., Polikarpov, I. & Craievich, A. F. (2004). Protein Sci. 13, 2825-2828.
13. Garci'a De La Torre, J., Huertas, M. L. & Carrasco, B. (2000). Biophys. J. 78, 719-730.
14. Gil, D. F., García-Fernández, R., Alonso-del-Rivero, M., Lamazares, E., Pé rez, M., Varas, L., Díaz, J., Chá vez, M. A., González-Gonzá lez, Y. & Mansur, M. (2011). FEMS Yeast Res. 11, 575-586.
15. Huber, R., Kukla, D., Bode, W., Schwager, P., Bartels, K., Deisenhofer, J. & Steigemann, W. (1974). J. Mol. Biol. 89, 73-101.
16. Kunitz, M. & Northrop, J. H. (1936). J. Gen. Physiol. 19, 991-1007.
17. Lafont, S., Veesler, S., Astier, J. P. & Boistelle, R. (1994). J. Cryst. Growth, 143, 249-255.
18. Laskowski, M. Jr, Qasim, M. A. & Lu, S. M. (2000). Protein-Protein Recognition, edited by C. Kleanthous, pp. 228-279. Oxford University Press
19. Leslie, A. G.W. & Powell, H. R. (2007). EvolvingMethods for Macromolecular Crystallography, edited by R. J. Read& J. L. Sussman, pp. 41-51. Dordrecht: Springer
20. Matthews, B. W. (1968). J. Mol. Biol. 33, 491-497.
21. 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.
22. Otting, G., Liepinsh, E. & Wüthrich, K. (1993). Biochemistry, 32, 3571-3582.
23. Petersen, L. C., Bjørn, S. E., Olsen, O. H., Nordfang, O., Norris, F. & Norris, K. (1996). Eur. J. Biochem. 235, 310-316.
24. Pritchard, L. & Dufton, M. J. (1999). J. Mol. Biol. 285, 1589-1607.
25. Redecke, L., Binder, S., Elmallah, M. I., Broadbent, R., Tilkorn, C., Schulz, B., May, P., Goos, A., Eich, A., Rübhausen, M. & Betzel, C. (2009). Free Radic. Biol. Med. 46, 1353-1361.
26. Scheidig, A. J., Hynes, T. R., Pelletier, L. A., Wells, J. A. & Kossiakoff, A. A. (1997). Protein Sci. 6, 1806-1824.
27. Tung, M. & Gallagher, D. T. (2009). Acta Cryst. D65, 18-23.
28. Vriend, G. (1990). J. Mol. Graph. 8, 52-56.
29. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
30. Wlodawer, A., Walter, J., Huber, R. & Sjölin, L. (1984). J. Mol. Biol. 180, 301-329.