1yo5
From Proteopedia
(New page: 200px<br /> <applet load="1yo5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yo5, resolution 2.00Å" /> '''Analysis of the 2.0...) |
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| - | [[Image:1yo5.gif|left|200px]]<br /> | + | [[Image:1yo5.gif|left|200px]]<br /><applet load="1yo5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1yo5" size=" | + | |
caption="1yo5, resolution 2.00Å" /> | caption="1yo5, resolution 2.00Å" /> | ||
'''Analysis of the 2.0A crystal structure of the protein-DNA complex of human PDEF Ets domain bound to the prostate specific antigen regulatory site'''<br /> | '''Analysis of the 2.0A crystal structure of the protein-DNA complex of human PDEF Ets domain bound to the prostate specific antigen regulatory site'''<br /> | ||
==Overview== | ==Overview== | ||
| - | PDEF, a prostate epithelial specific transcription factor, is a member of | + | PDEF, a prostate epithelial specific transcription factor, is a member of the Ets family of DNA binding proteins. Here we report a 2.0 A crystal structure of the PDEF Ets domain in complex with a natural, high-affinity DNA binding site in the promoter/enhancer region of the human prostate specific antigen gene. Comparison of the PDEF-DNA complex with other Ets complexes revealed key features that are shared among Ets members, as well as important differences in substrate specification at both the "GGA" core and the flanking regions of the DNA site. The combination of the serine residue at position 308 and the glutamine at position 311 explains the previous observation that the PDEF binds preferentially to a thymine at the +4 position of its binding site. Despite the common essential features that are shared among Ets members, PDEF demonstrates distinct patterns of interactions at different positions of DNA in achieving sequence specific recognition. Collectively, the common and unique interactions with both the DNA bases and the backbone phosphates lead to substrate specificity and individual preference for certain DNA sites. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1YO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YO5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Feng, L.]] | [[Category: Feng, L.]] | ||
[[Category: Ghosh, D.]] | [[Category: Ghosh, D.]] | ||
| - | [[Category: Gulick, A | + | [[Category: Gulick, A M.]] |
[[Category: Liu, Y.]] | [[Category: Liu, Y.]] | ||
[[Category: Said, M.]] | [[Category: Said, M.]] | ||
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[[Category: ets; protein-dna complex; double helix]] | [[Category: ets; protein-dna complex; double helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:07:21 2008'' |
Revision as of 14:07, 21 February 2008
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Analysis of the 2.0A crystal structure of the protein-DNA complex of human PDEF Ets domain bound to the prostate specific antigen regulatory site
Contents |
Overview
PDEF, a prostate epithelial specific transcription factor, is a member of the Ets family of DNA binding proteins. Here we report a 2.0 A crystal structure of the PDEF Ets domain in complex with a natural, high-affinity DNA binding site in the promoter/enhancer region of the human prostate specific antigen gene. Comparison of the PDEF-DNA complex with other Ets complexes revealed key features that are shared among Ets members, as well as important differences in substrate specification at both the "GGA" core and the flanking regions of the DNA site. The combination of the serine residue at position 308 and the glutamine at position 311 explains the previous observation that the PDEF binds preferentially to a thymine at the +4 position of its binding site. Despite the common essential features that are shared among Ets members, PDEF demonstrates distinct patterns of interactions at different positions of DNA in achieving sequence specific recognition. Collectively, the common and unique interactions with both the DNA bases and the backbone phosphates lead to substrate specificity and individual preference for certain DNA sites.
Disease
Known diseases associated with this structure: Alzheimer disease, type 3 OMIM:[104311], Alzheimer disease, type 3, with spastic paraparesis and apraxia OMIM:[104311], Alzheimer disease, type 3, with spastic paraparesis and unusual plaques OMIM:[104311], Cardiomyopathy, dilated, 1U OMIM:[104311], Dementia, frontotemporal OMIM:[104311], Pick disease OMIM:[104311]
About this Structure
1YO5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Analysis of the 2.0 A crystal structure of the protein-DNA complex of the human PDEF Ets domain bound to the prostate specific antigen regulatory site., Wang Y, Feng L, Said M, Balderman S, Fayazi Z, Liu Y, Ghosh D, Gulick AM, Biochemistry. 2005 May 17;44(19):7095-106. PMID:15882048
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