4CN5

Crystal Structure of the Human Retinoid X Receptor DNA-Binding Domain Bound to the Human Nr1d1 Response Element

4CN5 の概要

• エントリーDOI: 10.2210/pdb4cn5/pdb
• 関連するPDBエントリー: 4CN2 4CN3 4CN7
• 分子名称: RETINOIC ACID RECEPTOR RXR-ALPHA, 5'-D(*TP*GP*GP*GP*GP*TP*CP*AP*GP*AP*GP*TP*TP*CP *AP*AP*TP)-3', 5'-D(*AP*TP*TP*GP*AP*AP*CP*TP*CP*TP*GP*AP*CP*CP *CP*CP*AP)-3', ... (8 entities in total)
• 機能のキーワード: transcription-dna complex, transcription/dna
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Nucleus : P19793
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 31596.93

構造登録者

McEwen, A.G.,Poussin-Courmontagne, P.,Osz, J.,Rochel, N. (登録日: 2014-01-21, 公開日: 2015-02-18, 最終更新日: 2023-12-20)

主引用文献

Osz, J.,Mcewen, A.G.,Poussin-Courmontagne, P.,Moutier, E.,Birck, C.,Davidson, I.,Moras, D.,Rochel, N.
Structural Basis of Natural Promoter Recognition by the Retinoid X Nuclear Receptor.
Sci.Rep., 5:8216-, 2015

PubMed Abstract: Retinoid X receptors (RXRs) act as homodimers or heterodimerisation partners of class II nuclear receptors. RXR homo- and heterodimers bind direct repeats of the half-site (A/G)G(G/T)TCA separated by 1 nucleotide (DR1). We present a structural characterization of RXR-DNA binding domain (DBD) homodimers on several natural DR1s and an idealized symmetric DR1. Homodimers displayed asymmetric binding, with critical high-affinity interactions accounting for the 3' positioning of RXR in heterodimers on DR1s. Differing half-site and spacer DNA sequence induce changes in RXR-DBD homodimer conformation notably in the dimerization interface such that natural DR1s are bound with higher affinity than an idealized symmetric DR1. Subtle changes in the consensus DR1 DNA sequence therefore specify binding affinity through altered RXR-DBD-DNA contacts and changes in DBD conformation suggesting a general model whereby preferential half-site recognition determines polarity of heterodimer binding to response elements.

PubMed: 25645674
DOI: 10.1038/SREP08216

実験手法

X-RAY DIFFRACTION (2 Å)