1PDN

CRYSTAL STRUCTURE OF A PAIRED DOMAIN-DNA COMPLEX AT 2.5 ANGSTROMS RESOLUTION REVEALS STRUCTURAL BASIS FOR PAX DEVELOPMENTAL MUTATIONS

1PDN の概要

• エントリーDOI: 10.2210/pdb1pdn/pdb
• 分子名称: DNA (5'-D(*AP*AP*CP*GP*TP*CP*AP*CP*GP*GP*TP*TP*GP*AP*C)-3'), DNA (5'-D(*TP*TP*GP*TP*CP*AP*AP*CP*CP*GP*TP*GP*AP*CP*G)-3'), PROTEIN (PRD PAIRED), ... (4 entities in total)
• 機能のキーワード: protein-dna complex, double helix, pax, prd, paired domain, dna-binding protein, gene regulation-dna complex, gene regulation/dna
• 由来する生物種: Drosophila melanogaster (fruit fly)
• 細胞内の位置: Nucleus: P06601
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 23383.38

構造登録者

Xu, W.,Rould, M.A.,Jun, S.,Desplan, C.,Pabo, C.O. (登録日: 1995-05-16, 公開日: 1995-07-31, 最終更新日: 2024-02-14)

主引用文献

Xu, W.,Rould, M.A.,Jun, S.,Desplan, C.,Pabo, C.O.
Crystal structure of a paired domain-DNA complex at 2.5 A resolution reveals structural basis for Pax developmental mutations.
Cell(Cambridge,Mass.), 80:639-650, 1995

PubMed Abstract: The 2.5 A resolution structure of a cocrystal containing the paired domain from the Drosophila paired (prd) protein and a 15 bp site shows structurally independent N-terminal and C-terminal subdomains. Each of these domains contains a helical region resembling the homeodomain and the Hin recombinase. The N-terminal domain makes extensive DNA contacts, using a novel beta turn motif that binds in the minor groove and a helix-turn-helix unit with a docking arrangement surprisingly similar to that of the lambda repressor. The C-terminal domain is not essential for prd binding and does not contact the optimized site. All known developmental missense mutations in the paired box of mammalian Pax genes map to the N-terminal subdomain, and most of them are found at the protein-DNA interface.

PubMed: 7867071
DOI: 10.1016/0092-8674(95)90518-9

実験手法

X-RAY DIFFRACTION (2.5 Å)