2lef: Difference between revisions

Revision as of 18:58, 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:2lef.png

Template:STRUCTURE 2lef

LEF1 HMG DOMAIN (FROM MOUSE), COMPLEXED WITH DNA (15BP), NMR, 12 STRUCTURESLEF1 HMG DOMAIN (FROM MOUSE), COMPLEXED WITH DNA (15BP), NMR, 12 STRUCTURES

Template:ABSTRACT PUBMED 7651541

About this StructureAbout this Structure

2LEF is a Single protein structure of sequence from Mus musculus. This structure supersedes the now removed PDB entry 1lef. Full experimental information is available from OCA.

ReferenceReference

Structural basis for DNA bending by the architectural transcription factor LEF-1., Love JJ, Li X, Case DA, Giese K, Grosschedl R, Wright PE, Nature. 1995 Aug 31;376(6543):791-5. PMID:7651541

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

OCA

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 {{STRUCTURE_2lef|  PDB=2lef  |  SCENE=  }}
-'''LEF1 HMG DOMAIN (FROM MOUSE), COMPLEXED WITH DNA (15BP), NMR, 12 STRUCTURES'''
+===LEF1 HMG DOMAIN (FROM MOUSE), COMPLEXED WITH DNA (15BP), NMR, 12 STRUCTURES===
-==Overview==
+<!--
-Lymphoid enhancer-binding factor (LEF-1) and the closely related T-cell factor 1 (TCF-1) are sequence-specific and cell-type-specific DNA-binding proteins that play important regulatory roles in organogenesis and thymocyte differentiation. LEF-1 participates in regulation of the enhancer associated with the T cell receptor (TCR)-alpha gene by inducing a sharp bend in the DNA and facilitating interactions between Ets-1, PEBP2-alpha, and ATF/CREB, transcription factors bound at sites flanking the LEF-1 site. It seems that LEF-1 plays an architectural role in the assembly and function of this regulatory nucleoprotein complex. LEF-1 recognizes a specific nucleotide sequence through a high-mobility-group (HMG) domain. Proteins containing HMG domains bind DNA in the minor groove, bend the double helix, and recognize four-way junctions and other irregular DNA structures. Here we report the solution structure of a complex of the LEF-1 HMG domain and adjacent basic region with its cognate DNA. The structure reveals the HMG domain bound in the widened minor groove of a markedly distorted and bent double helix. The basic region binds across the narrowed major groove and contributes to DNA recognition.
+The line below this paragraph, {{ABSTRACT_PUBMED_7651541}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7651541 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7651541}}
 ==About this Structure==
-LEF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1lef 1lef]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LEF OCA].
+LEF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1lef 1lef]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LEF OCA].
 ==Reference==
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 [[Category: Tcr-a]]
 [[Category: Transcription factor]]
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