Open AccessPurification, crystallization and preliminary X‐ray diffraction of wild‐type and mutant recombinant human transforming growth factor β‐induced protein (TGFBIp)
Author(s) -
Runager Kasper,
GarcíaCastellanos Raquel,
Valnickova Zuzana,
Kristensen Torsten,
Nielsen Niels Chr.,
Klintworth Gordon K.,
GomisRüth F. Xavier,
Enghild Jan J.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109005016
Subject(s) - tgfbi , mutant , recombinant dna , extracellular matrix , transforming growth factor , mutant protein , transforming growth factor beta , extracellular , wild type , biology , chemistry , microbiology and biotechnology , gene , biochemistry
Transforming 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.