Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2ILX

Solution structure of catalytic domain of rat 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNP) protein

1N4T」から置き換えられました
2ILX の概要
エントリーDOI10.2210/pdb2ilx/pdb
関連するPDBエントリー1N4T 1WOJ 2I3E
NMR情報BMRB: 5202
分子名称2',3'-cyclic-nucleotide 3'-phosphodiesterase (1 entity in total)
機能のキーワードcnp, cnpase, nervous system, hydrolase
由来する生物種Rattus norvegicus (Norway rat)
細胞内の位置Membrane: P13233
タンパク質・核酸の鎖数1
化学式量合計24251.83
構造登録者
Denisov, A.Y.,Kozlov, G.,Gehring, K. (登録日: 2006-10-03, 公開日: 2007-03-06, 最終更新日: 2024-05-29)
主引用文献Kozlov, G.,Denisov, A.Y.,Pomerantseva, E.,Gravel, M.,Braun, P.E.,Gehring, K.
Solution structure of the catalytic domain of RICH protein from goldfish.
Febs J., 274:1600-1609, 2007
Cited by
PubMed Abstract: Regeneration-induced CNPase homolog (RICH) is an axonal growth-associated protein, which is induced in teleost fish upon optical nerve injury. RICH consists of a highly acidic N-terminal domain, a catalytic domain with 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) activity and a C-terminal isoprenylation site. In vitro RICH and mammalian brain CNPase specifically catalyze the hydrolysis of 2',3'-cyclic nucleotides to produce 2'-nucleotides, but the physiologically relevant in vivo substrate remains unknown. Here, we report the NMR structure of the catalytic domain of goldfish RICH and describe its binding to CNPase inhibitors. The structure consists of a twisted nine-stranded antiparallel beta-sheet surrounded by alpha-helices on both sides. Despite significant local differences mostly arising from a seven-residue insert in the RICH sequence, the active site region is highly similar to that of human CNPase. Likewise, refinement of the catalytic domain of rat CNPase using residual dipolar couplings gave improved agreement with the published crystal structure. NMR titrations of RICH with inhibitors point to a similar catalytic mechanism for RICH and CNPase. The results suggest a functional importance for the evolutionarily conserved phosphodiesterase activity and hint of a link with pre-tRNA splicing.
PubMed: 17480208
DOI: 10.1111/j.1742-4658.2007.05707.x
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2ilx
検証レポート(詳細版)ダウンロードをダウンロード

227561

件を2024-11-20に公開中

PDB statisticsPDBj update infoContact PDBjnumon