1dp7
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(New page: 200px<br /> <applet load="1dp7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dp7, resolution 1.5Å" /> '''COCRYSTAL STRUCTURE ...)
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Revision as of 14:28, 12 November 2007
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COCRYSTAL STRUCTURE OF RFX-DBD IN COMPLEX WITH ITS COGNATE X-BOX BINDING SITE
Overview
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.
About this Structure
1DP7 is a Single protein structure of sequence from [1] with EDO and PEG as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding., Gajiwala KS, Chen H, Cornille F, Roques BP, Reith W, Mach B, Burley SK, Nature. 2000 Feb 24;403(6772):916-21. PMID:10706293
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