2eze: Difference between revisions

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-[[Image:2eze.gif|left|200px]]<br />
-<applet load="2eze" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2eze" />
-'''SOLUTION STRUCTURE OF A COMPLEX OF THE SECOND 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==
+==SOLUTION STRUCTURE OF A COMPLEX OF THE SECOND DNA BINDING DOMAIN OF HUMAN HMG-I(Y) BOUND TO DNA DODECAMER CONTAINING THE PRDII SITE OF THE INTERFERON-BETA PROMOTER, NMR, 35 STRUCTURES==
-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.
+<StructureSection load='2eze' size='340' side='right'caption='[[2eze]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2eze]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EZE FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2eze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eze OCA], [https://pdbe.org/2eze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eze RCSB], [https://www.ebi.ac.uk/pdbsum/2eze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eze ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/HMGA1_HUMAN HMGA1_HUMAN] A chromosomal aberration involving HMGA1 is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with RAD51B.
+== Function ==
+[https://www.uniprot.org/uniprot/HMGA1_HUMAN HMGA1_HUMAN] HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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==
+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<ref>PMID:9253416</ref>
-Known diseases associated with this structure: Lipoma (1) OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600701 600701]]
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-EZE 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2EZE OCA].
+</div>
+<div class="pdbe-citations 2eze" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9253416 9253416]
+*[[High mobility group protein|High mobility group protein]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bewley, C.]]
+[[Category: Bewley C]]
-[[Category: Clore, G.M.]]
+[[Category: Clore GM]]
-[[Category: Gronenborn, A.M.]]
+[[Category: Gronenborn AM]]
-[[Category: Huth, J.R.]]
+[[Category: Huth JR]]
-[[Category: architectural factor]]
-[[Category: complex (dna-binding protein/dna)]]
-[[Category: dna binding protein]]
-[[Category: minor groove dna binding]]
-[[Category: transcriptional co-activator]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:57:36 2007''