1XPX

Structural basis of prospero-DNA interaction; implications for transcription regulation in developing cells

1XPX の概要

• エントリーDOI: 10.2210/pdb1xpx/pdb
• 分子名称: 5'-D(*AP*GP*CP*AP*TP*GP*CP*CP*TP*G)-3', 5'-D(*CP*AP*GP*GP*CP*AP*TP*GP*CP*T)-3', Protein prospero, ... (4 entities in total)
• 機能のキーワード: homeodomain, protein-dna binding, prospero, neural cell development, transcription regulation-dna complex, transcription regulation/dna
• 由来する生物種: Drosophila melanogaster (fruit fly)
• 細胞内の位置: Nucleus: P29617
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 25633.41

構造登録者

Yousef, M.S.,Matthews, B.W. (登録日: 2004-10-09, 公開日: 2005-05-03, 最終更新日: 2024-02-14)

主引用文献

Yousef, M.S.,Matthews, B.W.
Structural Basis of Prospero-DNA Interaction: Implications for Transcription Regulationin Developing Cells.
STRUCTURE, 13:601-607, 2005

PubMed Abstract: The crystal structure of a complex between the novel homeodomain of the neural transcription factor Prospero and DNA shows that the invariant residues Lys1290, Asn1294, and Asp1297 make specific contacts with the noncanonical DNA binding site. The overall structure includes the homeodomain and the adjacent Prospero domain and confirms that they act as a single structural unit, a Homeo-Prospero domain. The Prospero domain facilitates the proper alignment of the protein on the DNA. Knowledge of the structure reconciles two different DNA sequences that have been proposed as transcriptional targets for Prospero. As in the apo structure, the C terminus of the Prospero domain shields a short helix within the homeodomain that includes a nuclear export signal (NES). The structural results suggest that exposure of the NES is not coupled directly to DNA binding. We propose a DNA recognition mechanism specific to Prospero-type homeodomains in developing cells.

PubMed: 15837198
DOI: 10.1016/j.str.2005.01.023

実験手法

X-RAY DIFFRACTION (2.8 Å)