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Purification, crystallization and preliminary X-ray diffraction of wild-type and mutant recombinant human transforming growth factor β-induced protein (TGFBIp)

AuthorsRunager, Kasper; García-Castellanos, Raquel; Valnickova, Zuzana; Kristensen, Torsten Nygaard; Nielsen, Niels Chr.; Kintworth, Gordon K.; Gomis-Rüth, F. Xavier ; Enghild, Jan J.
KeywordsCorneal dystrophy
Recombinant protein
Issue DateMar-2009
PublisherInternational Union of Crystallography
CitationActa Crystallographica Section F: Structural Biology and Crystallization Communications 65(3): 299-303 (2009)
AbstractTransforming growth factor β-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. © 2009 International Union of Crystallography All rights reserved.
Publisher version (URL)http://dx.doi.org/10.1107/S1744309109005016
Identifiersdoi: 10.1107/S1744309109005016
issn: 1744-3091
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