2ezg: Difference between revisions
New page: left|200px<br /> <applet load="2ezg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ezg" /> '''SOLUTION STRUCTURE OF A COMPLEX OF THE THIR... |
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'''SOLUTION STRUCTURE OF A COMPLEX OF THE THIRD DNA BINDING DOMAIN OF HUMAN HMG-I(Y) BOUND TO DNA DODECAMER CONTAINING THE PRDII SITE OF THE INTERFERON-BETA PROMOTER, NMR, 35 STRUCTURES'''<br /> | '''SOLUTION STRUCTURE OF A COMPLEX OF THE THIRD DNA BINDING DOMAIN OF HUMAN HMG-I(Y) BOUND TO DNA DODECAMER CONTAINING THE PRDII SITE OF THE INTERFERON-BETA PROMOTER, NMR, 35 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
The solution structure of a complex between a truncated form of HMG-I(Y), consisting of the second and third DNA binding domains (residues 51-90), and a DNA dodecamer containing the PRDII site of the interferon-beta | The solution structure of a complex between a truncated form of HMG-I(Y), consisting of the second and third DNA binding domains (residues 51-90), and a DNA dodecamer containing the PRDII site of the interferon-beta promoter has been solved by multidimensional nuclear magnetic resonance spectroscopy. The stoichiometry of the complex is one molecule of HMG-I(Y) to two molecules of DNA. The structure reveals a new architectural minor groove binding motif which stabilizes B-DNA, thereby facilitating the binding of other transcription factors in the opposing major groove. The interactions involve a central Arg-Gly-Arg motif together with two other modules that participate in extensive hydrophobic and polar contracts. The absence of one of these modules in the third DNA binding domain accounts for its-100 fold reduced affinity relative to the second one. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
2EZG 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:// | 2EZG 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=2EZG OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bewley, C.]] | [[Category: Bewley, C.]] | ||
[[Category: Clore, G | [[Category: Clore, G M.]] | ||
[[Category: Gronenborn, A | [[Category: Gronenborn, A M.]] | ||
[[Category: Huth, J | [[Category: Huth, J R.]] | ||
[[Category: architectural factor]] | [[Category: architectural factor]] | ||
[[Category: complex (dna-binding protein/dna)]] | [[Category: complex (dna-binding protein/dna)]] | ||
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[[Category: transcriptional co-activator]] | [[Category: transcriptional co-activator]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:04 2008'' | ||
Revision as of 18:16, 21 February 2008
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SOLUTION STRUCTURE OF A COMPLEX OF THE THIRD DNA BINDING DOMAIN OF HUMAN HMG-I(Y) BOUND TO DNA DODECAMER CONTAINING THE PRDII SITE OF THE INTERFERON-BETA PROMOTER, NMR, 35 STRUCTURES
OverviewOverview
The solution structure of a complex between a truncated form of HMG-I(Y), consisting of the second and third DNA binding domains (residues 51-90), and a DNA dodecamer containing the PRDII site of the interferon-beta promoter has been solved by multidimensional nuclear magnetic resonance spectroscopy. The stoichiometry of the complex is one molecule of HMG-I(Y) to two molecules of DNA. The structure reveals a new architectural minor groove binding motif which stabilizes B-DNA, thereby facilitating the binding of other transcription factors in the opposing major groove. The interactions involve a central Arg-Gly-Arg motif together with two other modules that participate in extensive hydrophobic and polar contracts. The absence of one of these modules in the third DNA binding domain accounts for its-100 fold reduced affinity relative to the second one.
DiseaseDisease
Known diseases associated with this structure: Lipoma (1) OMIM:[600701]
About this StructureAbout this Structure
2EZG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif., Huth JR, Bewley CA, Nissen MS, Evans JN, Reeves R, Gronenborn AM, Clore GM, Nat Struct Biol. 1997 Aug;4(8):657-65. PMID:9253416
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