1dp7
From Proteopedia
(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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- | [[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=" | + | |
caption="1dp7, resolution 1.5Å" /> | caption="1dp7, resolution 1.5Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Burley, S K.]] |
[[Category: Chen, H.]] | [[Category: Chen, H.]] | ||
[[Category: Cornille, F.]] | [[Category: Cornille, F.]] | ||
- | [[Category: Gajiwala, K | + | [[Category: Gajiwala, K S.]] |
[[Category: Mach, B.]] | [[Category: Mach, B.]] | ||
[[Category: Reith, W.]] | [[Category: Reith, W.]] | ||
- | [[Category: Roques, B | + | [[Category: Roques, B P.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: PEG]] | [[Category: PEG]] | ||
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[[Category: winged helix]] | [[Category: winged helix]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:01 2008'' |
Revision as of 10:19, 21 February 2008
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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 and 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
Page seeded by OCA on Thu Feb 21 12:19:01 2008