Chemical basis for the affinity maturation of a camel single domain antibody

Journal of Biological Chemistry

Volumn 279, Issue 51, 2004, Pages 53593-53601

  De Genst, Erwin ^a   Handelberg, Fabian ^a   Van Meirhaeghe, Annemieke ^a   Vynck, Samuel ^a   Loris, Remy ^a   Wyns, Lode ^a   Muyldermans, Serge ^a  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGENS; CRYSTAL STRUCTURE; ENTROPY; HYDROGEN BONDS; HYDROPHOBICITY; ISOMERS; LIVING SYSTEMS STUDIES; PLASTICITY; SOLVENTS;

AFFINITY MATURATION; HEAVY-CHAIN ANTIBODIES; REACTIVE GERM LINE CONFORMATIONAL ISOMER; TRANSITION STATES;

ANTIBODIES;

AMINO ACID; HYDROGEN; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; LYSOZYME; MUTANT PROTEIN; SERINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTIBODY AFFINITY; ANTIGEN BINDING; ARTICLE; ARTIODACTYLA; COMPLEMENTARITY DETERMINING REGION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENERGY; ENTHALPY; ENTROPY; GERM LINE; HYDROGEN BOND; HYDROPHOBICITY; ISOMER; KINETICS; MOLECULE; PLASTICITY; PRECURSOR; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROCESSING; PROTEIN STABILITY; SOLVATION; SOMATIC HYPERMUTATION;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; ANTIBODY AFFINITY; ANTIGEN-ANTIBODY REACTIONS; BASE SEQUENCE; BINDING SITES, ANTIBODY; CAMELS; CHICKENS; COMPLEMENTARITY DETERMINING REGIONS; CRYSTALLOGRAPHY, X-RAY; ENTROPY; GENES, IMMUNOGLOBULIN; HEAT; HYDROGEN BONDING; IMMUNOGLOBULIN VARIABLE REGION; KINETICS; LYSINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MURAMIDASE; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, NUCLEIC ACID; SERINE; TEMPERATURE; THERMODYNAMICS;

ARTIODACTYLA; CAMELIDAE; CAMELUS DROMEDARIUS;

EID: 11144241270     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M407843200     Document Type: Article

References (33)

1. Padlan, E. A. (1996) Adv. Prot. Chem. 49, 57-133
2. Milstein, C., and Neuberger, M. S. (1996) Adv. Prot. Chem. 49, 451-485
3. Neuberger, M. S., Ehrenstein, M. R., Klix, N., Jolly, C. J., Yelamos, J., Rada, C., and Milstein, C. (1998) Immunol. Rev. 162, 107-116
4. Weill, J. C., and Reynaud, C. A. (1996) Immunol. Today 17, 92-97
5. Wedemayer, G. J., Patten, P. A., Wang, L. H., Schultz, P. G., and Stevens, R. C. (1997) Science 276, 1665-1669
6. Manivel, V., Sahoo, N. C., Salunke, D. M., and Rao, K. V. (2000) Immunity 13, 611-620
7. Li, Y., Li, H., Yang, F., Smith-Gill, S. J., and Mariuzza, R. A. (2003) Nat. Struct. Biol. 10, 482-488
8. Muyldermans, S., Cambillau, C., and Wyns, L. (2001) Trends Biochem. Sci. 26, 230-235
9. Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hamers, C., Songa, E. B., Bendahman, N., and Hamers, R. (1993) Nature 363, 446-448
10. Nguyen, V. K., Hamers, R., Wyns, L., and Muyldermans, S. (2000) EMBO J. 19, 921-930
11. Decanniere, K., Transue, T. R., Desmyter, A., Maes, D., Muyldermans, S., and Wyns, L. (2001) J. Mol. Biol. 313, 473-478
12. Desmyter, A., Transue, T. R., Ghahroudi, M. A., Dao-Thi, M. H., Poortmans, F., Hamers, R., Muyldermans, S., and Wyns, L. (1996) Nat. Struct. Biol. 3, 803-811
13. Ghahroudi, M. A., Desmyter, A., Wyns, L., Hamers, R., and Muyldermans, S. (1997) FEBS Lett. 414, 521-526
14. Lauwereys, M., Ghahroudi, M. A., Desmyter, A., Kinne, J., Holzer, W., De Genst, E., Wyns, L., and Muyldermans, S. (1998) BMBO J. 17, 3512-3520
15. Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) Prot. Sci. 4, 2411-2423
16. De Genst, E., Areskough, D., Decanniere, K., Muyldermans, S., and Andersson K. (2001) J. Biol. Chem. 277, 29897-29907
17. Ito, W., Yasui, H., and Kurosawa, Y. (1995) J. Mol. Biol. 248, 729-732
18. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
19. Navaza, J. (1994) Acta Crystallogr. Sect A 50, 157-163
20. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Acta Crystallogr. Sect. D Biol. Crystallogr. 54, 905-921
21. Kabat, E. A., Wu, T. T., Perry, H. M., Gottesman, K. S., and Foeler, C. (1991) Sequences of Proteins of Immunological Interest, US Public Health Services
22. Karlsson, R., and Fält, A. (1997) J. Immunol. Methods 200, 121-133
23. Tomlinson, I. M., Walter, G., Jones, P. T., Dear, P. H., Sonnhammer, E. L., and Winter, G. (1996) J. Mol. Biol. 256, 813-817
24. Lo Conte, L., Chothia, C., and Janin, J. (1999) J. Mol. Biol. 285, 2177-2198
25. Boniface, J. J., Reich, Z., Lyons, D. S., and Davis, M. M. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 11446-11451
26. Decanniere, K., Muyldermans, S., and Wyns, L. (2000) J. Mol. Biol. 300, 83-91
27. Chothia, C., Lesk, A. M., Tramontane, A., Levitt, M., Smith-Gill, S. J., Air, G., Sheriff, S., Padlan, E. A., Davies, D., and Tulip, W. R., Colman, P. M., Alzari, P. M., and Poljak, R. J. (1989) Nature 342, 877-883
28. Chong, L. T., Duan, Y., Wang, L., Massova, I., and Kollman, P. A. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 14330-14335
29. Yang, P. L., and Schultz, P. G. (1999) J. Mol. Biol. 294, 1191-1201
30. Sundberg, E. J., and Mariuzza, R. A. (2003) Adv. Prot. Chem. 61, 119-160
31. Cauerhff, A., Goldbaum, F. A., and Braden, B. C. (2004) Proc. Natl. Acad. Sci. U. S. A. 101, 3539-3544
32. Bond, C. J., Marsters, J. C., and Sidhu, S. S. (2003) J. Mol. Biol. 332, 643-655
33. Jones, S., and Thornton, J. M. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 13-20