1CTL

STRUCTURE OF THE CARBOXY-TERMINAL LIM DOMAIN FROM THE CYSTEINE RICH PROTEIN CRP

1CTL の概要

• エントリーDOI: 10.2210/pdb1ctl/pdb
• 分子名称: AVIAN CYSTEINE RICH PROTEIN, ZINC ION (2 entities in total)
• 機能のキーワード: lim domain containing proteins, metal-binding protein, metal binding protein
• 由来する生物種: Gallus gallus (chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8969.96

構造登録者

Perez-Alvarado, G.C.,Miles, C.,Michelsen, J.W.,Louis, H.A.,Winge, D.R.,Beckerle, M.C.,Summers, M.F. (登録日: 1995-01-06, 公開日: 1995-06-03, 最終更新日: 2024-05-22)

主引用文献

Perez-Alvarado, G.C.,Miles, C.,Michelsen, J.W.,Louis, H.A.,Winge, D.R.,Beckerle, M.C.,Summers, M.F.
Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRP.
Nat.Struct.Biol., 1:388-398, 1994

PubMed Abstract: The three dimensional solution structure of the carboxy terminal LIM domain of the avian Cysteine Rich Protein (CRP) has been determined by nuclear magnetic resonance spectroscopy. The domain contains two zinc atoms bound independently in CCHC (C = Cys, H = His) and CCCC modules. Both modules contain two orthogonally-arranged antiparallel beta-sheets, and the CCCC module contains an alpha-helix at its C terminus. The modules pack due to hydrophobic interactions forming a novel global fold. The structure of the C-terminal CCCC module is essentially identical to that observed for the DNA-interactive CCCC modules of the GATA-1 and steroid hormone receptor DNA binding domains, raising the possibility that the LIM motif may have a DNA binding function.

PubMed: 7664053
DOI: 10.1038/nsb0694-388

実験手法

SOLUTION NMR