1DP7
COCRYSTAL STRUCTURE OF RFX-DBD IN COMPLEX WITH ITS COGNATE X-BOX BINDING SITE
Summary for 1DP7
Entry DOI | 10.2210/pdb1dp7/pdb |
Descriptor | DNA (5'-D(*CP*GP*(BRU)P*TP*AP*CP*CP*AP*(BRU)P*GP*GP*TP*AP*AP*CP*G)-3'), MHC CLASS II TRANSCRIPTION FACTOR HRFX1, 1,2-ETHANEDIOL, ... (5 entities in total) |
Functional Keywords | winged helix, mhc class ii transcription factor, protein-dna cocrystal structure, novel mode of dna recognition, transcription-dna complex, transcription/dna |
Total number of polymer chains | 2 |
Total formula weight | 14087.27 |
Authors | Gajiwala, K.S.,Chen, H.,Cornille, F.,Roques, B.P.,Reith, W.,Mach, B.,Burley, S.K. (deposition date: 1999-12-23, release date: 2000-03-06, Last modification date: 2024-02-07) |
Primary citation | Gajiwala, K.S.,Chen, H.,Cornille, F.,Roques, B.P.,Reith, W.,Mach, B.,Burley, S.K. Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding. Nature, 403:916-921, 2000 Cited by PubMed Abstract: Regulatory factor X (RFX) proteins are transcriptional activators that recognize X-boxes (DNA of the sequence 5'-GTNRCC(0-3N)RGYAAC-3', where N is any nucleotide, R is a purine and Y is a pyrimidine) using a highly conserved 76-residue DNA-binding domain (DBD). DNA-binding defects in the protein RFX5 cause bare lymphocyte syndrome or major histocompatibility antigen class II deficiency. RFX1, -2 and -3 regulate expression of other medically important gene products (for example, interleukin-5 receptor alpha chain, IL-5R alpha). Fusions of the ligand-binding domain of the oestrogen receptor with the DBD of RFX4 occur in some human breast tumours. Here we present a 1.5 A-resolution structure of two copies of the DBD of human RFX1 (hRFX1) binding cooperatively to a symmetrical X-box. hRFX1 is an unusual member of the winged-helix subfamily of helix-turn-helix proteins because it uses a beta-hairpin (or wing) to recognize DNA instead of the recognition helix typical of helix-turn-helix proteins. A new model for interactions between linker histones and DNA is proposed. PubMed: 10706293DOI: 10.1038/35002634 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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