2LY4: High mobility group protein B1

HMGB1-facilitated p53 DNA binding occurs via HMG-box/p53 transactivation domain interaction and is regulated by the acidic tail. Determined by solution NMR. Released 31 Oct 2012.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 1,053
Mol. weight: 19.69 kDa
Released: 31 Oct 2012

Explore 2LY4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2LY4 contains 4 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	14-29	16
α-helix	37-49	13
α-helix	53-75	23

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	47-50	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
High mobility group protein B1	A	protein	83	Homo sapiens	P09429 (AlphaFold model)
Cellular tumor antigen p53	B	protein	93	Homo sapiens	P04637 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2LY4_1 High mobility group protein B1 (chains A)
GKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFE
DMAKADKARYEREMKTYIPPKGE

Sequence of entity 2 (B), FASTA

>2LY4_2 Cellular tumor antigen p53 (chains B)
MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGP
DEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPL

Primary citation

HMGB1-Facilitated p53 DNA Binding Occurs via HMG-Box/p53 Transactivation Domain Interaction, Regulated by the Acidic Tail. Rowell, J.P., Simpson, K.L., Stott, K. et al. Structure (2012) 20:2014-2024. DOI 10.1016/j.str.2012.09.004 · PubMed

Other PDB entries of the same protein (UniProt P09429 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9CG9 2.94 Å, Cryo-EM structure of an HMGB1 box bound to nucleosome at SHL-2
6CIK 3.15 Å, Pre-Reaction Complex, RAG1(E962Q)/2-intact/nicked 12/23RSS complex in Mn2+
6CG0 3.17 Å, Cryo-EM structure of mouse RAG1/2 HFC complex (3.17 A)
6CIM 3.6 Å, Pre-Reaction Complex, RAG1(E962Q)/2-nicked/intact 12/23RSS complex in Mn2+
6OEM 3.6 Å, Cryo-EM structure of mouse RAG1/2 PRC complex (DNA0)
6OEO 3.69 Å, Cryo-EM structure of mouse RAG1/2 NFC complex (DNA1)
6CIJ 3.9 Å, Cryo-EM structure of mouse RAG1/2 HFC complex containing partial HMGB1 linker(3.9 A)
6CIL 4.15 Å, Pre-reaction complex, RAG1(E962Q)/2-intact/intact 12/23RSS complex in MN2+
6OEN 4.3 Å, Cryo-EM structure of mouse RAG1/2 PRC complex (DNA1)
8I9M 5.19 Å, The RAGE and HMGB1 complex
2RTU Solution structure of oxidized human HMGB1 A box
2YRQ Solution structure of the tandem HMG box domain from Human High mobility group protein B1

Browse structure collections

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