1pue: Difference between revisions
New page: left|200px<br /><applet load="1pue" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pue, resolution 2.100Å" /> '''PU.1 ETS DOMAIN-DNA... |
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[[Image:1pue.gif|left|200px]]<br /><applet load="1pue" size=" | [[Image:1pue.gif|left|200px]]<br /><applet load="1pue" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1pue, resolution 2.100Å" /> | caption="1pue, resolution 2.100Å" /> | ||
'''PU.1 ETS DOMAIN-DNA COMPLEX'''<br /> | '''PU.1 ETS DOMAIN-DNA COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
The Ets family of transcription factors, of which there are now about 35 | The Ets family of transcription factors, of which there are now about 35 members regulate gene expression during growth and development. They share a conserved domain of around 85 amino acids which binds as a monomer to the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal structure of an ETS domain complexed with DNA, at 2.3-A resolution. The domain is similar to alpha + beta (winged) 'helix-turn-helix' proteins and interacts with a ten-base-pair region of duplex DNA which takes up a uniform curve of 8 degrees. The domain contacts the DNA by a novel loop-helix-loop architecture. Four of amino acids that directly interact with the DNA are highly conserved: two arginines from the recognition helix lying in the major groove, one lysine from the 'wing' that binds upstream of the core GGAA sequence, and another lysine, from the 'turn' of the 'helix-turn-helix' motif, which binds downstream and on the opposite strand. | ||
==About this Structure== | ==About this Structure== | ||
1PUE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | 1PUE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Klemsz, M.]] | [[Category: Klemsz, M.]] | ||
[[Category: Kodandapani, R.]] | [[Category: Kodandapani, R.]] | ||
[[Category: Maki, R | [[Category: Maki, R A.]] | ||
[[Category: McKercher, S.]] | [[Category: McKercher, S.]] | ||
[[Category: Ni, C | [[Category: Ni, C Z.]] | ||
[[Category: Piccialli, G.]] | [[Category: Piccialli, G.]] | ||
[[Category: Pio, F.]] | [[Category: Pio, F.]] | ||
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[[Category: transforming protein]] | [[Category: transforming protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:38 2008'' |
Revision as of 15:32, 21 February 2008
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PU.1 ETS DOMAIN-DNA COMPLEX
OverviewOverview
The Ets family of transcription factors, of which there are now about 35 members regulate gene expression during growth and development. They share a conserved domain of around 85 amino acids which binds as a monomer to the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal structure of an ETS domain complexed with DNA, at 2.3-A resolution. The domain is similar to alpha + beta (winged) 'helix-turn-helix' proteins and interacts with a ten-base-pair region of duplex DNA which takes up a uniform curve of 8 degrees. The domain contacts the DNA by a novel loop-helix-loop architecture. Four of amino acids that directly interact with the DNA are highly conserved: two arginines from the recognition helix lying in the major groove, one lysine from the 'wing' that binds upstream of the core GGAA sequence, and another lysine, from the 'turn' of the 'helix-turn-helix' motif, which binds downstream and on the opposite strand.
About this StructureAbout this Structure
1PUE is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex., Kodandapani R, Pio F, Ni CZ, Piccialli G, Klemsz M, McKercher S, Maki RA, Ely KR, Nature. 1996 Apr 4;380(6573):456-60. PMID:8602247
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