PDBsum entry: 2ell

Gene regulation

PDB id: 2ell

Contents

Protein chain

168 a.a. *

* Residue conservation analysis

PDB id:

2ell

Name:

Gene regulation

Title:

Solution structure of the leucine rich repeat of human acidi rich nuclear phosphoprotein 32 family member b

Structure:

Acidic leucine-rich nuclear phosphoprotein 32 fam b. Chain: a. Fragment: lrr_1 domain. Synonym: phapi2 protein, silver-stainable protein ssp29, ac protein rich in leucines. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: anp32b. Other_details: cell-free protein synthesis

NMR struc:

20 models

Authors:

N.Tochio,S.Koshiba,S.Watanabe,T.Harada,T.Umehara,A.Tanaka,T. S.Yokoyama,Riken Structural Genomics/proteomics Initiative

Key ref:

N.Tochio et al. (2010). Solution structure of histone chaperone ANP32B: Interaction with core histones H3-H4 through its acidic concave domain. J Mol Biol, 401, 97-114. PubMed id: 20538007 DOI: 10.1016/j.jmb.2010.06.005

Date:

27-Mar-07 Release date: 01-Apr-08

Protein chain

Q92688  (AN32B_HUMAN) -  Acidic leucine-rich nuclear phosphoprotein 32 family member B

Seq: 251 a.a.

Struc: 168 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: protein binding (1 term)

DOI no: 10.1016/j.jmb.2010.06.005

J Mol Biol 401:97-114 (2010)

PubMed id: 20538007

Solution structure of histone chaperone ANP32B: Interaction with core histones H3-H4 through its acidic concave domain.

N.Tochio, T.Umehara, Y.Munemasa, T.Suzuki, S.Sato, K.Tsuda, S.Koshiba, T.Kigawa, R.Nagai, S.Yokoyama.

ABSTRACT

Eukaryotic gene expression is regulated by histone deposition onto and eviction from nucleosomes, which are mediated by several chromatin-modulating factors. Among them, histone chaperones are key factors that facilitate nucleosome assembly. Acidic nuclear phosphoprotein 32B (ANP32B) belongs to the ANP32 family, which shares N-terminal leucine-rich repeats (LRR) and a C-terminal variable anionic region. The C-terminal region functions as an inhibitor of histone acetylation, but the functional roles of the LRR domain in chromatin regulation have remained elusive. Here we report that the LRR domain of ANP32B possesses histone chaperone activity, and forms a curved structure with a parallel beta-sheet on the concave side and mostly helical elements on the convex side. Our analyses revealed that the interaction of ANP32B with the core histones H3-H4 occurs on its concave side, and both the acidic and hydrophobic residues that compose the concave surface are critical for the histone-binding. These results provide a structural framework for understanding the functional mechanisms of acidic histone chaperones.