This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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 ...) |
|||
| Line 1: | Line 1: | ||
| - | [[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]] | ||
| Line 27: | Line 26: | ||
[[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
|
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
