”@
 
”@

Reference

1. Mach, B., Steimle, V., Martinez-Soria, E. & Reith, W. Regulation of MHC class II genes: lessons from a disease. Annu. Rev. Immunol. 14, 301-331 (1996). 
2. Iwama, A. et al. Dimeric RFX proteins contribute to the activity and lineage speciRcity of the interleukin-5 receptor alpha promoter through activation and repression domains. Mol. Cell Biol. 19, 3940-3950 (1999). 
3. Dotzlaw, H., Alkhalaf, M. & Murphy, L. C. Characterization of estrogen receptor variant mRNAs from human breast cancers. Mol. Endocrinol. 6, 773-785 (1992). 
4. Reith, W. et al. MHC class II regulatory factor RFX has a novel DNA-binding domain and a functionally independent dimerization domain. Genes Dev. 4, 1528-1540 (1990). 
5. Cornille, F. et al. DNA binding properties of a chemically synthesized DNA binding domain of hRFX1. Nucleic Acids Res. 26, 2143-2149 (1998). 
6. Clark, K. L., Halay, E. D., Lai, E. & Burley, S. K. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature 364, 412-420 (1993). 
7. Lai, E., Clark, K. L., Burley, S. & James E. Darnell, J. Hepatocyte nuclear factor 3/fork head or ``winged helix'' proteins: A family of transcription factors of diverse biological function. Proc. Natl Acad. Sci. USA 90, 10421-10423 (1993). 
8. Emery, P. et al. Aconsensus motif in the RFX DNAbinding domain and binding domain mutants with altered speciRcity. Mol. Cell Biol. 16, 4486-4494 (1996). 
9. Ostapchuk, P., Scheirle, G. & Hearing, P. Binding of nuclear factor EF-C to a functional domain of the hepatitis B virus enhancer region. Mol. Cell Biol. 9, 2787-2797 (1989). 
10. Jin, C., Marsden, I., Chen, X. & Liao, X. Dynamic DNA contacts observed in the NMR structure of winged helix protein-DNA complex. J. Mol. Biol. 289, 683-690 (1999). 
11. Zheng, N., Fraenkel, E., Pabo, C. O. & Pavletich, N. P. Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP. Genes Dev. 13, 666-674 (1999). 
12. Janin, J. Principles of protein-protein recognition from structure to thermodynamics. Biochimie 77, 497-505 (1995). 
13. Reith, W. et al. RFX1, a transactivator of hepatitis B virus enhancer I, belongs to a novel family of homodimeric and heterodimeric DNA-binding proteins. Mol. Cell Biol. 14, 1230-1244 (1994). 
14. Lavery, R. & Sklenar, H. The deRnition of generalized helicoidal parameters and of axis curvature for irregular nucleic acids. J. Biomol. Struct. Dynamics 6, 63-91 (1988). 
15. Klemm, J. D. & Pabo, C. O. Oct-1 POU domain-DNA interactions: cooperative binding of isolated subdomains and effects of covalent linkage. Genes Dev. 10, 27-36 (1996). 
16. Ramakrishnan, V., Finch, J., Graziano, V. & Sweet, R. Crystal structure of the globular domain of histone H5 and its implications for nucleosome binding. Nature 362, 219-223 (1993). 
17. Thomas, J. O. & Wilson, C. M. Selective radiolabelling and identiRcation of a strong nucleosome binding site on the globular domain of histone H5. EMBO J. 5, 3531-3537 (1986). 
18. Buckle, R. S., Maman, J. D. & Allan, J. Site-directed mutagenesis studies on the binding of the globular domain of linker histone H5 to the nucleosome. J. Mol. Biol. 223, 651-659 (1992). 
19. Holm, L. & Sander, C. Families of structurally similar proteins, version 1. 0. J. Mol. Biol. 233, 123-138 (1993). 
20. Goytisolo, F. A. et al. IdentiRcation of two DNA-binding sites on the globular domain of histone H5. EMBO J. 15, 3421-3429 (1996). 
21. Cirillo, L. A. et al. Binding of the winged-helix transcription factor HNF3 to a linker histone site on the nucleosome. EMBO J. 17, 244-254 (1998). 
22. Zhou, Y. B., Gerchman, S. E., Ramakrishnan, V., Travers, A. & Muyldermans, S. Position and orientation of the globular domain of linker histone H5 on the nucleosome. Nature 395, 402-405 (1998). 
23. Brunger, A. T. et al. Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998). 
24. Laskowski, R. J., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-290 (1993). 
25. Nicholls, A., Sharp, K. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).