5L3O

Crystal Structure of Human Carbonic Anhydrase II in Complex with a Quinoline Oligoamide Foldamer

これはPDB形式変換不可エントリーです。

5L3O の概要

• エントリーDOI: 10.2210/pdb5l3o/pdb
• 分子名称: Carbonic anhydrase 2, Aromatic foldamer, ZINC ION, ... (5 entities in total)
• 機能のキーワード: protein-foldamer complex, protein foldamer interactions, modified inhibitor, anchored foldamer, hcaii dimerisation, quinoline oligoamide foldamer, benzene sulfonamide modified inhibitor, lyase-inhibitor complex, lyase/inhibitor
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 64703.08

構造登録者

Jewginski, M.,Langlois d'Estaintot, B.,Granier, T.,Huc, Y. (登録日: 2016-05-24, 公開日: 2017-03-01, 最終更新日: 2024-11-20)

主引用文献

Jewginski, M.,Granier, T.,Langlois d'Estaintot, B.,Fischer, L.,Mackereth, C.D.,Huc, I.
Self-Assembled Protein-Aromatic Foldamer Complexes with 2:3 and 2:2:1 Stoichiometries.
J. Am. Chem. Soc., 139:2928-2931, 2017

PubMed Abstract: The promotion of protein dimerization using the aggregation properties of a protein ligand was explored and shown to produce complexes with unusual stoichiometries. Helical foldamer 2 was synthesized and bound to human carbonic anhydrase (HCA) using a nanomolar active site ligand. Crystal structures show that the hydrophobicity of 2 and interactions of its side chains lead to the formation of an HCA-2 complex in which three helices of 2 are stacked, two of them being linked to an HCA molecule. The middle foldamer in the stack can be replaced by alternate sequences 3 or 5. Solution studies by CD and NMR confirm left-handedness of the helical foldamers as well as HCA dimerization.

PubMed: 28170240
DOI: 10.1021/jacs.7b00184

実験手法

X-RAY DIFFRACTION (1.98 Å)