1MM3

Solution structure of the 2nd PHD domain from Mi2b with C-terminal loop replaced by corresponding loop from WSTF

1MM3 の概要

• エントリーDOI: 10.2210/pdb1mm3/pdb
• 関連するPDBエントリー: 1f62 1FP0 1MM2
• NMR情報: BMRB: 5556
• 分子名称: Mi2-beta(Chromodomain helicase-DNA-binding protein 4) and transcription factor WSTF, ZINC ION (2 entities in total)
• 機能のキーワード: phd, zinc finger, protein scaffold, dna binding protein-transcription complex, dna binding protein/transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q14839
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6905.65

構造登録者

Kwan, A.H.Y.,Gell, D.A.,Verger, A.,Crossley, M.,Matthews, J.M.,Mackay, J.P. (登録日: 2002-09-02, 公開日: 2003-07-22, 最終更新日: 2024-05-29)

主引用文献

Kwan, A.H.Y.,Gell, D.A.,Verger, A.,Crossley, M.,Matthews, J.M.,Mackay, J.P.
Engineering a Protein Scaffold from a PHD Finger
structure, 11:803-813, 2003

PubMed Abstract: The design of proteins with tailored functions remains a relatively elusive goal. Small size, a well-defined structure, and the ability to maintain structural integrity despite multiple mutations are all desirable properties for such designer proteins. Many zinc binding domains fit this description. We determined the structure of a PHD finger from the transcriptional cofactor Mi2beta and investigated the suitability of this domain as a scaffold for presenting selected binding functions. The two flexible loops in the structure were mutated extensively by either substitution or expansion, without affecting the overall fold of the domain. A binding site for the corepressor CtBP2 was also grafted onto the domain, creating a new PHD domain that can specifically bind CtBP2 both in vitro and in the context of a eukaryotic cell nucleus. These results represent a step toward designing new regulatory proteins for modulating aberrant gene expression in vivo.

PubMed: 12842043
DOI: 10.1016/S0969-2126(03)00122-9

実験手法

SOLUTION NMR