2KFT

NMR Solution structure of the first PHD finger domain of human Autoimmune Regulator (AIRE) in complex with Histone H3(1-20Cys) Peptide

2KFT の概要

• エントリーDOI: 10.2210/pdb2kft/pdb
• NMR情報: BMRB: 16878
• 分子名称: Autoimmune regulator, Histone H3, ZINC ION (3 entities in total)
• 機能のキーワード: phd finger, histone code, aire, apeced, transcription, alternative splicing, cytoplasm, disease mutation, dna-binding, metal-binding, nucleus, phosphoprotein, polymorphism, transcription regulation, zinc, zinc-finger, chromosomal protein, nucleosome core, transcription-protein binding complex, transcription/protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: O43918
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8444.36

構造登録者

Chakravarty, S.,Zeng, L.,Zhou, M. (登録日: 2009-02-27, 公開日: 2009-04-28, 最終更新日: 2024-05-22)

主引用文献

Chakravarty, S.,Zeng, L.,Zhou, M.M.
Structure and Site-Specific Recognition of Histone H3 by the PHD Finger of Human Autoimmune Regulator.
Structure, 17:670-679, 2009

PubMed Abstract: Human autoimmune regulator (AIRE) functions to control thymic expression of tissue-specific antigens via sequence-specific histone H3 recognition by its plant homeodomain (PHD) finger. Mutations in the AIRE PHD finger have been linked to autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED). Here we report the three-dimensional solution structure of the first PHD finger of human AIRE bound to a histone H3 peptide. The structure reveals a detailed network of interactions between the protein and the amino-terminal residues of histone H3, and particularly key electrostatic interactions of a conserved aspartic acid 297 in AIRE with the unmodified lysine 4 of histone H3 (H3K4). NMR binding study with H3 peptides carrying known posttranslational modifications flanking H3K4 confirms that transcriptional regulation by AIRE through its interactions with histone H3 is confined to the first N-terminal eight residues in H3. Our study offers a molecular explanation for the APECED mutations and helps define a subclass of the PHD finger family proteins that recognize histone H3 in a sequence-specific manner.

PubMed: 19446523
DOI: 10.1016/j.str.2009.02.017

実験手法

SOLUTION NMR