2KFT
NMR Solution structure of the first PHD finger domain of human Autoimmune Regulator (AIRE) in complex with Histone H3(1-20Cys) Peptide
Summary for 2KFT
| Entry DOI | 10.2210/pdb2kft/pdb |
| NMR Information | BMRB: 16878 |
| Descriptor | Autoimmune regulator, Histone H3, ZINC ION (3 entities in total) |
| Functional Keywords | 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 |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: O43918 |
| Total number of polymer chains | 2 |
| Total formula weight | 8444.36 |
| Authors | Chakravarty, S.,Zeng, L.,Zhou, M. (deposition date: 2009-02-27, release date: 2009-04-28, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 19446523DOI: 10.1016/j.str.2009.02.017 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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