7PO9

Crystal structure of ZAD-domain of M1BP protein from D.melanogaster

7PO9 の概要

• エントリーDOI: 10.2210/pdb7po9/pdb
• 分子名称: LD30467p, ZINC ION (3 entities in total)
• 機能のキーワード: zinc-finger associated domain, zad, protein interaction, dimerization, m1bp, 9797, zinc binding, treble-cleft-like, transcription
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22190.64

構造登録者

Boyko, K.M.,Bonchuk, A.N.,Nikolaeva, A.Y.,Georgiev, P.G.,Popov, V.O. (登録日: 2021-09-08, 公開日: 2021-12-08, 最終更新日: 2024-06-19)

主引用文献

Bonchuk, A.N.,Boyko, K.M.,Nikolaeva, A.Y.,Burtseva, A.D.,Popov, V.O.,Georgiev, P.G.
Structural insights into highly similar spatial organization of zinc-finger associated domains with a very low sequence similarity.
Structure, 30:1004-, 2022

PubMed Abstract: ZAD is a C4 zinc-coordinating domain often found at the N-terminus mostly of arthropodan transcription factors with multiple C2H2 zinc-finger domains involved in the regulation of chromosome architecture and promotor activity. ZADs predominantly form homodimers and have low primary sequence similarity. We obtained three crystal structures of the most phylogenetically distant Drosophila ZADs and structure of the only known ZAD-like domain from a mammalian protein (ZNF276). All ZAD structures demonstrate unity of the spatial fold as well as some unique structural features. The specific homodimerization of ZAD is primarily determined by the position and size of secondary structural elements and is further strengthened by a number of unique interactions between subunits. Structural comparison allowed for unraveling key sequence features underlying the similarity of the spatial fold. These features result in a broad variety of ZADs in Arthropod C2H2 proteins, allowing for the emergence of a wide range of highly specific homodimers.

PubMed: 35580610
DOI: 10.1016/j.str.2022.04.009

実験手法

X-RAY DIFFRACTION (1.9 Å)