Runager Kasper, García-Castellanos Raquel, Valnickova Zuzana, Kristensen Torsten, Nielsen Niels Chr, Klintworth Gordon K, Gomis-Rüth F Xavier, Enghild Jan J
Center for Insoluble Protein Structures and Interdisciplinary Nanoscience Center at the Department of Molecular Biology, University of Aarhus, Denmark.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt 3):299-303. doi: 10.1107/S1744309109005016. Epub 2009 Feb 26.
Transforming growth factor beta-induced protein (TGFBIp) has been linked to several corneal dystrophies as certain point mutations in the protein may give rise to a progressive accumulation of insoluble protein material in the human cornea. Little is known about the biological functions of this extracellular protein, which is expressed in various tissues throughout the human body. However, it has been found to interact with a number of extracellular matrix macromolecules such as collagens and proteoglycans. Structural information about TGFBIp might prove to be a valuable tool in the elucidation of its function and its role in corneal dystrophies caused by mutations in the TGFBI gene. A simple method for the purification of wild-type and mutant forms of recombinant human TGFBIp from human cells under native conditions is presented here. Moreover, the crystallization and preliminary X-ray analysis of TGFBIp are reported.
转化生长因子β诱导蛋白（TGFBIp）与多种角膜营养不良有关，因为该蛋白中的某些点突变可能导致人类角膜中不溶性蛋白质物质的渐进性积累。关于这种在人体各种组织中表达的细胞外蛋白的生物学功能知之甚少。然而，已发现它能与多种细胞外基质大分子相互作用，如胶原蛋白和蛋白聚糖。关于TGFBIp的结构信息可能是阐明其功能以及它在由TGFBI基因突变引起的角膜营养不良中所起作用的宝贵工具。本文介绍了一种在天然条件下从人细胞中纯化重组人TGFBIp野生型和突变型的简单方法。此外，还报道了TGFBIp的结晶及初步X射线分析。
