PDBsum entry 2ruz

Transcription

PDB id: 2ruz

Contents

Protein chain

38 a.a.

Metals

_ZN

PDB id:

2ruz

Name:

Transcription

Title:

Solution structures of the DNA-binding domain (zf11) of immune-related zinc-finger protein zfat

Structure:

Zinc finger protein zfat. Chain: a. Fragment: unp residues 796-826. Synonym: zinc finger gene in aitd susceptibility region, zinc finger protein 406. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: zfat, kiaa1485, zfat1, znf406. Expressed in: cell-free synthesis.

NMR struc:

20 models

Authors:

N.Tochio,T.Umehara,T.Kigawa,S.Yokoyama

Key ref:

N.Tochio et al. (2015). Solution structures of the DNA-binding domains of immune-related zinc-finger protein ZFAT. J Struct Funct Genomics, 16, 55-65. PubMed id: 25801860 DOI: 10.1007/s10969-015-9196-3

Date:

26-Jan-15 Release date: 08-Apr-15

Protein chain

Q9P243  (ZFAT_HUMAN) -  Zinc finger protein ZFAT from Homo sapiens

Seq: 1243 a.a.

Struc: 38 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DOI no: 10.1007/s10969-015-9196-3

J Struct Funct Genomics 16:55-65 (2015)

PubMed id: 25801860

Solution structures of the DNA-binding domains of immune-related zinc-finger protein ZFAT.

N.Tochio, T.Umehara, K.Nakabayashi, M.Yoneyama, K.Tsuda, M.Shirouzu, S.Koshiba, S.Watanabe, T.Kigawa, T.Sasazuki, S.Shirasawa, S.Yokoyama.

ABSTRACT

ZFAT is a transcriptional regulator, containing eighteen C2H2-type zinc-fingers and one AT-hook, involved in autoimmune thyroid disease, apoptosis, and immune-related cell survival. We determined the solution structures of the thirteen individual ZFAT zinc-fingers (ZF) and the tandemly arrayed zinc-fingers in the regions from ZF2 to ZF5, by NMR spectroscopy. ZFAT has eight uncommon bulged-out helix-containing zinc-fingers, and six of their structures (ZF4, ZF5, ZF6, ZF10, ZF11, and ZF13) were determined. The distribution patterns of the putative DNA-binding surface residues are different among the ZFAT zinc-fingers, suggesting the distinct DNA sequence preferences of the N-terminal and C-terminal zinc-fingers. Since ZFAT has three to five consecutive tandem zinc-fingers, which may cooperatively function as a unit, we also determined two tandemly arrayed zinc-finger structures, between ZF2 to ZF4 and ZF3 to ZF5. Our NMR spectroscopic analysis detected the interaction between ZF4 and ZF5, which are connected by an uncommon linker sequence, KKIK. The ZF4-ZF5 linker restrained the relative structural space between the two zinc-fingers in solution, unlike the other linker regions with determined structures, suggesting the involvement of the ZF4-ZF5 interfinger linker in the regulation of ZFAT function.