2LEF

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

Replaces:  1LEF

Summary for 2LEF

• Entry DOI: 10.2210/pdb2lef/pdb
• NMR Information: BMRB: 4248
• Descriptor: DNA (5'-D(*CP*AP*CP*CP*CP*TP*TP*TP*GP*AP*AP*GP*CP*TP*C)-3'), DNA (5'-D(*GP*AP*GP*CP*TP*TP*CP*AP*AP*AP*GP*GP*GP*TP*G)-3'), PROTEIN (LYMPHOID ENHANCER-BINDING FACTOR) (3 entities in total)
• Functional Keywords: lef1, hmg, tcr-a, transcription factor, dna binding, dna bending, complex (hmg domain-dna), gene regulation-dna complex, gene regulation/dna
• Biological source: Mus musculus (house mouse)
• Cellular location: Nucleus: P27782
• Total number of polymer chains: 3
• Total formula weight: 19582.20

Authors

Li, X.,Love, J.J.,Case, D.A.,Wright, P.E. (deposition date: 1998-10-13, release date: 1998-10-21, Last modification date: 2023-12-27)

Primary citation

Love, J.J.,Li, X.,Case, D.A.,Giese, K.,Grosschedl, R.,Wright, P.E.
Structural basis for DNA bending by the architectural transcription factor LEF-1.
Nature, 376:791-795, 1995

PubMed Abstract: 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.

PubMed: 7651541
DOI: 10.1038/376791a0

Experimental method

SOLUTION NMR