4UUS

CRYSTAL STRUCTURE OF A UBX-EXD-DNA COMPLEX INCLUDING THE UBDA MOTIF

4UUS の概要

• エントリーDOI: 10.2210/pdb4uus/pdb
• 関連するPDBエントリー: 4UUT
• 分子名称: HOMEOTIC PROTEIN ULTRABITHORAX, HOMEOTIC PROTEIN EXTRADENTICLE, 5'-D(*GP*TP*CP*GP*CP*CP*AP*TP*AP*AP*AP*TP*CP*AP*C)-3', ... (5 entities in total)
• 機能のキーワード: transcription, homeodomain, hox protein, pbc protein, dna protein complex, transcription factor
• 由来する生物種: DROSOPHILA MELANOGASTER (FRUIT FLY); 詳細
• 細胞内の位置: Nucleus: P83949 P40427
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 55254.01

構造登録者

Foos, N.,Mate, M.J.,Ortiz-Lombardia, M. (登録日: 2014-07-31, 公開日: 2015-02-18, 最終更新日: 2024-01-10)

主引用文献

Foos, N.,Maurel-Zaffran, C.,Mate, M.J.,Vincentelli, R.,Hainaut, M.,Berenger, H.,Pradel, J.,Saurin, A.J.,Ortiz-Lombardia, M.,Graba, Y.
A Flexible Extension of the Drosophila Ultrabithorax Homeodomain Defines a Novel Hox/Pbc Interaction Mode.
Structure, 23:270-, 2015

PubMed Abstract: The patterning function of Hox proteins relies on assembling protein complexes with PBC proteins, which often involves a protein motif found in most Hox proteins, the so-called Hexapeptide (HX). Hox/PBC complexes likely gained functional diversity by acquiring additional modes of interaction. Here, we structurally characterize the first HX alternative interaction mode based on the paralogue-specific UbdA motif and further functionally validate structure-based predictions. The UbdA motif folds as a flexible extension of the homeodomain recognition helix and defines Hox/PBC contacts that occur, compared with those mediated by the HX motif, on the opposing side of the DNA double helix. This provides a new molecular facet to Hox/PBC complex assembly and suggests possible mechanisms for the diversification of Hox protein function.

PubMed: 25651060
DOI: 10.1016/J.STR.2014.12.011

実験手法

X-RAY DIFFRACTION (2.55 Å)