Subunit association and conformational flexibility in the head subdomain of human CD81 large extracellular loop

Biological Chemistry

Volumn 383, Issue 9, 2002, Pages 1447-1452

  Kitadokoro, Kengo ^a   Ponassi, Marco ^a   Galli, Giuliano ^a   Petracca, Roberto ^a   Falugi, Fabiana ^a   Grandi, Guido ^a   Bolognesi, Martino ^a  

^a UNIVERSITY OF GENOA   (Italy)

Author keywords

CD81; HCV E2 glycoprotein; Hepatitis C virus; Receptor protein; Tetraspanins

Indexed keywords

CD81 ANTIGEN; PROTEIN SUBUNIT; TETRASPANIN; VIRUS ENVELOPE PROTEIN; LEUKOCYTE ANTIGEN; MEMBRANE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HEPATITIS C VIRUS; HUMAN; HUMAN CELL; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PLIABILITY; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

HEPATITIS C VIRUS;

AMINO ACID SEQUENCE; ANTIGENS, CD; CRYSTALLOGRAPHY, X-RAY; HEPACIVIRUS; HUMANS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLIABILITY; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0036755086     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2002.164     Document Type: Article

References (28)

1. Berman, H. M., Westbrook, J., Feng, Z., Gilliland, G., Bhat, T. N., Weissig, H., Shindyalov, I. N. and Bourne, P. E. (2000) The Protein Data Bank. Nucleic Acids Res. 28, 235-242.
2. Boucheix, C. and Rubinstein, E. (2001). Tetraspanins. Cell Mol. Life Sci. 58, 1189-1205.
3. Brunger, 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. et al. (1998). Crystallography and NMR system (CNS): a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921.
4. Engh, R. and Huber, R. (1991). Accurate bond and angle parameters for X-ray structure refinement. Acta Crystallogr. A 47, 392-400.
5. Jones, T. A., Zou, J. -Y., Cowan, S. W. and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
6. Higginbottom, A., Quinn, E. R., Kuo, C. C., Flint, M., Wilson, L. H., Bianchi, E., Nicosia, A., Monk, P. N., McKeating, J. A. and Levy, S. (2000). Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2. J. Virol. 74, 3642-3649.
7. Hotta, H., Ross, A. H., Huebner, K., Isobe, M., Wendeborn, S., Chao, M. V., Ricciardi, R. P., Tsuijmoto, Y., Croce, C. M. and Koprowsky, H. (1998). Molecular cloning and characterization of an antigen associated with early stages of melanoma tumor progression. Cancer Res. 48, 2955-2962.
8. Kaji, K., Oda, S., Shikano, T., Ohnuki, T., Uematsu, Y., Sakagami, J., Tada, N., Miyazaki, S. and Kudo, A. (2000). The gamete fusion process is defective in eggs of CD9-deficient mice. Nature Genet. 24, 279-282.
9. Kissinger, C. R., Gehlhaar, D. K. and Fogel, D. B. (1999). Molecular replacement by evolutionary search. Acta Crystallogr. D 55, 484-491.
10. Kitadokoro, K., Bordo D., Galli, G., Petracca, R., Falugi, F., Abrignani S., Grandi, G. and Bolognesi, M. (2000a). CD81 extracellular domain 3D structure: insight into the tetraspanin superfamily structural motifs. EMBO J. 20, 12-18.
11. Kitadokoro, K., Galli, G., Petracca, R., Falugi, F., Grandi, G. and Bolognesi, M. (2000b). Crystallization and preliminary crystallographic studies on the large extracellular domain of human CD81, a tetraspanin receptor for hepatitis C virus. Acta Crystallogr. D 57, 156-158.
12. Kraulis, P. J. (1991). Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
13. Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993). PROCHECK: a program to check the stereo-chemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
14. Le Naour, F., Rubinstein, E., Jasmin, C., Prenant, M. and Boucheix, C. (2000). Severely reduced female fertility in CD9-deficient mice. Science 287, 319-321.
15. Levy, S., Todd, S. C. and Maecker, H. T. (1998). CD81 (TAPA-1): a molecule involved in signal transduction and cell adhesion in the immune system. Annu. Rev. Immunol. 16, 89-109.
16. Maecker, H. T., Todd, S. C. and Levy, S. (1997). The tetraspanin superfamily: molecular facilitators. FASEB J. 11, 428-442.
17. Matthews, B.W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
18. Merritt, E. A. and Murphy, M. E. P. (1994). Raster3D version 2.0 - a program for photorealistic molecular graphics. Acta Crystallogr. D 50, 869-873.
19. Miyado, K, Yamada, G., Yamada, S., Hasuwa, H., Nakamura, Y., Ryu, F., Suzuki, K., Kosai, K., Inoue, K., Ogura, A., Okabe, M. and Mekada, E. (2000). Requirement of CD9 on the egg plasma membrane for fertilization. Science 287, 321-324.
20. Miyake, M., Nakano, K., Ieky, Y., Adachi, M., Huang, C.L., Itoi, S., Koh, T. and Taki, T. (1995). Motility related protein 1 (MRP-1/CD9) expression: inverse correlation with metastases in breast cancer. Cancer Res. 55, 4127-4131.
21. Murshudov, G. N, Vagin, A. A. and Dodson, E. J. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255.
22. Otwinoski, Z. and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
23. Petracca, R., Falugi, F., Galli, G., Norais, N., Rosa, D., Campagnoli, S., Burgio, V., Di, Stasio, E., Giardina, B., Houghton, M., Abrignani, S. and Grandi, G. (2000). Structure-function analysis of hepatitis C virus envelope-CD81 binding. J. Virol. 74, 4824-4830.
24. Pileri, P., Uematsu, Y., Campagnoli, S., Galli, G., Falugi, F., Petracca, R., Weiner, A. J., Houghton, M., Rosa, D., Grandi, G. and Abrignani, S. (1998). Binding of hepatitis C virus to CD81. Science 282, 938-941.
25. Rice, C.M. (1999). Is CD81 the key to hepatitis C virus entry? Hepatology 29, 990-992.
26. Seigneuret, M., Delaguillaumie, A., Lagaudriere-Gesbert, C., and Conjeaud, H. (2001). Structure of the tetraspanin main extracellular domain. A partially conserved fold with a structurally variable domain insertion. J. Biol. Chem. 276, 40055-40064.
27. Testa, J. E., Brooks, P. C., Lin, J. M. and Quigley, J. P. (1999). Eukaryotic expression cloning with an antimetastatic monoclonal antibody identifies a tetraspanin (PETA-3/CD151) as an effector of human tumor cell migration and metastasis. Cancer Res. 59, 3812-3820.
28. Zemni, R., Bienvenu, T., Vinet, M. C., Sefiani, A., Carrie, A., Billuart, P. McDonell, N., Couvert, P., Francis, F., Chafey, P. et al. (2000). A new gene involved in X-linked mental retardation identified by analysis of an X;2 balanced translocation. Nature Genet. 24, 167-170.