1dp7: Difference between revisions

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New page: left|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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[[Image:1dp7.gif|left|200px]]<br />
[[Image:1dp7.gif|left|200px]]<br /><applet load="1dp7" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1dp7" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1dp7, resolution 1.5&Aring;" />
caption="1dp7, resolution 1.5&Aring;" />
'''COCRYSTAL STRUCTURE OF RFX-DBD IN COMPLEX WITH ITS COGNATE X-BOX BINDING SITE'''<br />
'''COCRYSTAL STRUCTURE OF RFX-DBD IN COMPLEX WITH ITS COGNATE X-BOX BINDING SITE'''<br />


==Overview==
==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.
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==
==About this Structure==
1DP7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with EDO and PEG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DP7 OCA].  
1DP7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DP7 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10706293 10706293]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10706293 10706293]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Burley, S.K.]]
[[Category: Burley, S K.]]
[[Category: Chen, H.]]
[[Category: Chen, H.]]
[[Category: Cornille, F.]]
[[Category: Cornille, F.]]
[[Category: Gajiwala, K.S.]]
[[Category: Gajiwala, K S.]]
[[Category: Mach, B.]]
[[Category: Mach, B.]]
[[Category: Reith, W.]]
[[Category: Reith, W.]]
[[Category: Roques, B.P.]]
[[Category: Roques, B P.]]
[[Category: EDO]]
[[Category: EDO]]
[[Category: PEG]]
[[Category: PEG]]
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[[Category: winged helix]]
[[Category: winged helix]]


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