1PDN

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

Summary for 1PDN

• Entry DOI: 10.2210/pdb1pdn/pdb
• Descriptor: 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)
• Functional Keywords: protein-dna complex, double helix, pax, prd, paired domain, dna-binding protein, gene regulation-dna complex, gene regulation/dna
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Nucleus: P06601
• Total number of polymer chains: 3
• Total formula weight: 23383.38

Authors

Xu, W.,Rould, M.A.,Jun, S.,Desplan, C.,Pabo, C.O. (deposition date: 1995-05-16, release date: 1995-07-31, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)