Camelid heavy-chain variable domains provide efficient combining sites to haptens

Biochemistry

Volumn 39, Issue 6, 2000, Pages 1217-1222

  Spinelli, Silvia ^a   Frenken, Leon G J ^b   Hermans, Pim ^b   Verrips, Theo ^b   Brown, Kieron ^a   Tegoni, Mariella ^a   Cambillau, Christian ^a  

^a Centre National de la Recherche Scientifique   (France)

^b UNILEVER RESEARCH VLAARDINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

HAPTEN;

AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANTIBODY PRODUCING CELL; ARTICLE; ARTIODACTYLA; BINDING AFFINITY; BINDING SITE; CRYSTAL STRUCTURE; MALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CAMELIDS, NEW WORLD; COLORING AGENTS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; HAPTENS; IMMUNOGLOBULIN HEAVY CHAINS; IMMUNOGLOBULIN VARIABLE REGION; MALE; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; TRIAZINES;

ANIMALIA; ARTIODACTYLA; CAMELIDAE; LAMA GLAMA;

EID: 0034673109     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991830w     Document Type: Article

References (32)

1. Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hamers, C., Songa, E. B., Bendahman, N., Hamers, R. (1993) Nature 363, 446-448.
2. Ghahroudi, M. A., Desmyter, A., Wyns, L., Hamers, R., and Muyldermans, S. (1997) FEBS Lett. 414, 521-526.
3. Franken, L., Hamers, R, Hamers-Casterman, C., Muyldermans, S., and Verrips, T. (1994) Production of antibodies or (functionalized) fragments thereof derived from heavy chain immunoglobulines of CAMELIDAE., patent number WO 94/ 25591.
4. Vu, K. B., Ghahroudi, M. A., Wyns, L., and Muyldermans, S. (1997) Mol. Immunol. 34, 1121-1131.
5. Desmyter, A., Transue, T. R., Ghahroudi, M. A., Thi, M. H., Poortmans, F., Hamers, R., Muyldermans, S., Wyns, L. (1996) Nature Struct. Biol. 3, 803-811.
6. Decanniere, K., Desmyter, A., Lauwereys, M., Ghahroudi, M. A., Muyldermans, S., Wyns, L. (1999) Structure 7, 361-370.
7. Spinelli, S., Frenken, L., Bourgeois, D., de Ron, L., Bos, W., Verrips, T., Anguille, C., Cambillau, C., and Tegoni, M. (1996) Nature Struct. Biol. 3, 752-756.
8. Transue, T. R., De Genst, E., Gharhroudi, M. A., Wyns, L., and Muyldermans, S. (1998) Proteins 32, 515-522.
9. Lauwereys, M., Arbabi Ghahroudi, M., Desmyter, A., Kinne, J., Holzer, W., De Genst, E., Wyns, L., Muyldermans, S. (1998) EMBO J. 17, 3512-3520.
10. Alzari, P. M., Spinelli, S., Mariuzza, R. A., Boulot, G., Poljak, R. J., Jarvis, J. M., and Milstein, C. (1990) EMBO J. 9, 3807-3814.
11. Wilson, I. A., and Stanfield, R. L. (1994) Curr. Opin. Struct. Biol. 4, 857-867.
12. HH antibody fragments and their high level secretion by Saccharomyces cerevisiae. J. Biotech., in press.
13. Otwinowski, Z., Minor, W. (1997) Methods Enzymol. 276, 307.
14. Collaborative Computational Project, No.4. (1994) Acta Crystallogr. D 50, 760.
15. Sheldrick, G. M. (1990) Acta Crystallogr. A 46, 467.
16. Navaza, J. (1994) Acta Crystallogr. A 50, 157.
17. Roussel, A., Cambillau, C. (1989) in Silicon Graphics Geometry partner directory (Fall 1989) (Silicon Graphics, Ed.) pp 77-78. Mountain View, California.
18. Brunger, A. T., Kuriyan, J., Karplus, M. (1987) Science 35, 458.
19. Brunger, A. T. (1996) XPLOR version 3.843 Manual. New Haven, Connecticut: Yale University Press.
20. Laskowski, R., MacArthur, M., Moss, D., and Thornton, J. (1993) J. Appl. Crystallogr. 26, 91.
21. Chothia, C., Lesk, A. M., Tramontano, A., Levitt, M., Smith-Gill, S. J., Air, G., Sheriff, S., Padlan, E. A., Davies, D., Tulip, W. R., Colman, P. M., Spinelli, S., Alzari, P. M., and Poljak, R. (1989) Nature 342, 877-883.
22. Martin, A. C., Thornton, J. M. (1996) J. Mol. Biol. 263, 800-815.
23. Al-Lazikani, B., Lesk, A. M., Chothia, C. (1997) J. Mol. Biol. 273, 927-948.
24. Mariuzza, R. A., Poljak, R. J., and Schwarz, F. P. (1994) Res. Immunol. 145, 70-72.
25. Malby, R. L., Tulip, W. R., Harley, V. R., KcKimm-Breschkin, J. L., Laver, W. G., Webster, R. G., and Colman, P. M. (1994) Structure 2, 733.
26. Webster, D. M., Henry, A. H., and Rees, A. R. (1994) Curr. Opin. Struct. Biol. 4, 123.
27. Trinh, C. H., Hemmington, S. D., Verhoeyen, M. E., and Phillips, S. E. V. (1997) Structure 5, 937.
28. Arevalo, J. H., Stura, E. A., Taussig, M. J., and Wilson, I. A. (1993) J. Mol. Biol. 231, 103.
29. Jeffrey, P. D., Strong, R. K., Sieker, L. C., Chang, C. Y., Campbell, R. L., Petsko, G. A., Haber, E., Margolies, M. N., Sheriff, S. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 10310-10314.
30. Quilez, R., de Lauzon, S., Desfosses, B., Mansuy, D., and Mahy, J. P. (1996) FEBS Lett 395, 73.
31. Kabat, E. A., Wu, T. T., Perry, H. M., Gottesman, K. S., Foeller, C. (1991) ed. 5, Bethesda, National Institute of Health.
32. Nichols, A. (1991) Proteins: Struct. Funct. Genet. 11, 281.