Phage display reveals a novel interaction of human tear lipocalin and thioredoxin which is relevant for ligand binding

被引:29
作者
Redl, B [1 ]
Merschak, P [1 ]
Abt, B [1 ]
Wojnar, P [1 ]
机构
[1] Univ Innsbruck, Fak Med, Inst Mikrobiol, A-6020 Innsbruck, Austria
基金
奥地利科学基金会;
关键词
protein-protein interaction; phage display; lipocalin; retinoic acid binding; von Ebner's gland protein;
D O I
10.1016/S0014-5793(99)01331-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Human tear lipocalin (TL) is an unusual member of the lipocalin protein family, since it is known to bind a large variety of lipophilic ligands in vivo and acts as a cysteine proteinase inhibitor in vitro, It is suggested to function as a physiological protection factor by scavenging lipophilic potentially harmful compounds. Since protein-protein interaction or macromolecular complexation is a common feature of many lipocalins, we applied phage display technology to identify TL interacting proteins, By panning of a human prostate cDNA phagemid library against purified TL me isolated a thioredoxin (Trx) encoding phage clone, Biochemical analysis revealed that TL indeed interacts with Trx and is reduced by this redox protein. Reduction of the TL-specific disulfide bond is of functional relevance, since the reduced protein shows a nine-fold increase in ligand affinity when tested with retinoic acid as ligand, (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:182 / 186
页数:5
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