1LO2

Retro-Diels-Alderase Catalytic Antibody

1LO2 の概要

• エントリーDOI: 10.2210/pdb1lo2/pdb
• 関連するPDBエントリー: 1L00 1L04 1L06
• 分子名称: If kappa light chain, Ig gamma 2a heavy chain, [2'-CARBOXYLETHYL]-10-METHYL-ANTHRACENE ENDOPEROXIDE, ... (4 entities in total)
• 機能のキーワード: catalytic antibody, fab, retro-diels-alderase, immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 96540.28

構造登録者

Hugot, M.,Reymond, J.L.,Baumann, U. (登録日: 2002-05-06, 公開日: 2002-06-26, 最終更新日: 2024-10-30)

主引用文献

Hugot, M.,Bensel, N.,Vogel, M.,Reymond, M.T.,Stadler, B.,Reymond, J.L.,Baumann, U.
A structural basis for the activity of retro-Diels-Alder catalytic antibodies: evidence for a catalytic aromatic residue.
Proc.Natl.Acad.Sci.USA, 99:9674-9678, 2002

PubMed Abstract: The nitroxyl synthase catalytic antibodies 10F11, 9D9, and 27C5 catalyze the release of nitroxyl from a bicyclic pro-drug by accelerating a retro-Diels-Alder reaction. The Fabs (antigen-binding fragments) of these three catalytic antibodies were cloned and sequenced. Fab 9D9 was crystallized in the apo-form and in complex with one transition state analogue of the reaction. Crystal structures of Fab 10F11 in complex with ligands mimicking substrate, transition state, and product have been determined at resolutions ranging from 1.8 to 2.3 A. Antibodies 9D9 and 10F11 show increased shape complementarity (as quantified by the program sc) to the hapten and to a modeled transition state as compared with substrate and product. The shape complementarity is mediated to a large extent by an aromatic residue (tyrosine or tryptophan) at the bottom of the hydrophobic active pocket, which undergoes pi-stacking interactions with the aromatic rings of the ligands. Another factor contributing to the different reactivity of the regioisomers probably arises because of hydrogen-bonding interactions between the nitroxyl bridge and the backbone amide of PheH101 and possibly a conserved water molecule.

PubMed: 12093912
DOI: 10.1073/pnas.142286599

実験手法

X-RAY DIFFRACTION (2 Å)