2ezg: Difference between revisions

Revision as of 05:37, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ezg.png

Template:STRUCTURE 2ezg

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 STRUCTURESSOLUTION 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

Template:ABSTRACT PUBMED 9253416

About this StructureAbout this Structure

2EZG is a Single protein structure of sequence from Homo sapiens. Full experimental 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

Page seeded by OCA on Mon Jul 28 05:36:58 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2ezg.gif|left|200px]]
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 {{STRUCTURE_2ezg|  PDB=2ezg  |  SCENE=  }}
-'''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'''
+===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===
-==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 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9253416}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9253416 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9253416}}
 ==About this Structure==
-EZG is a [[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].
+EZG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZG OCA].
 ==Reference==
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 [[Category: Minor groove dna binding]]
 [[Category: Transcriptional co-activator]]
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