2ADR

ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES

2ADR の概要

• エントリーDOI: 10.2210/pdb2adr/pdb
• 分子名称: ADR1, ZINC ION (2 entities in total)
• 機能のキーワード: transcription regulation, adr1, zinc finger
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P07248
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7257.01

構造登録者

Bowers, P.M.,Kleivt, R.E. (登録日: 1998-03-20, 公開日: 1998-06-17, 最終更新日: 2024-05-22)

主引用文献

Bowers, P.M.,Schaufler, L.E.,Klevit, R.E.
A folding transition and novel zinc finger accessory domain in the transcription factor ADR1.
Nat.Struct.Biol., 6:478-485, 1999

PubMed Abstract: The region responsible for sequence-specific DNA binding by the transcription factor ADR1 contains two Cys2-His2 zinc fingers and an additional N-terminal proximal accessory region (PAR). The N-terminal (non-finger) PAR is unstructured in the absence of DNA and undergoes a folding transition on binding the DNA transcription target site. We have used a set of HN-HN NOEs derived from a perdeuterated protein-DNA complex to describe the fold of ADR1 bound to the UAS1 binding site. The PAR forms a compact domain consisting of three antiparallel strands that contact A-T base pairs in the major groove. The three-strand domain is a novel fold among all known DNA-binding proteins. The PAR shares sequence homology with the N-terminal regions of other zinc finger proteins, suggesting that it represents a new DNA-binding module that extends the binding repertoire of zinc finger proteins.

PubMed: 10331877
DOI: 10.1038/8283

実験手法

SOLUTION NMR