2RR6

Solution structure of the leucine rich repeat of human acidic leucine-rich nuclear phosphoprotein 32 family member B

Summary for 2RR6

• Entry DOI: 10.2210/pdb2rr6/pdb
• Related: 2ell
• Descriptor: Acidic leucine-rich nuclear phosphoprotein 32 family member B (1 entity in total)
• Functional Keywords: phapi2 protein, silver-stainable protein ssp29, acidic protein rich in leucines, gene regulation, rdc
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Nucleus. Isoform 2: Cytoplasm: Q92688
• Total number of polymer chains: 1
• Total formula weight: 18842.56

Authors

Tochio, N.,Umehara, T.,Tsuda, K.,Koshiba, S.,Harada, T.,Watanabe, S.,Tanaka, A.,Kigawa, T.,Yokoyama, S. (deposition date: 2010-05-25, release date: 2010-06-09, Last modification date: 2024-05-01)

Primary citation

Tochio, N.,Umehara, T.,Munemasa, Y.,Suzuki, T.,Sato, S.,Tsuda, K.,Koshiba, S.,Kigawa, T.,Nagai, R.,Yokoyama, S.
Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain.
J.Mol.Biol., 401:97-114, 2010

PubMed 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 (LRRs) 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 histone binding. These results provide a structural framework for understanding the functional mechanisms of acidic histone chaperones.

PubMed: 20538007
DOI: 10.1016/j.jmb.2010.06.005

Experimental method

SOLUTION NMR