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Título: | Structural and functional implications of human transforming growth factor b-Induced protein, TGFBIp, in corneal dystrophies |
Autor: | García-Castellanos, Raquel CSIC ORCID; Sukusu Nielsen, Nadia; Runager, Kasper; Thøgersen, Ida B.; Lukassen, Marie V.; Poulsen, Ebbe T.; Goulas, Theodoros CSIC ORCID; Enghild, Jan J.; Gomis-Rüth, F. Xavier CSIC ORCID | Palabras clave: | Corneal dystrophy Fasciclin FAS1 domain Cysteine-rich CROPT domain Crystal structures Multi-domain protein Pathological mutants Extracellular matrix protein |
Fecha de publicación: | 7-nov-2017 | Editor: | Elsevier | Citación: | Structure 25(11): 1740-1750.e2 (2017) | Resumen: | A major cause of visual impairment, corneal dystrophies result from accumulation of protein deposits in the cornea. One of the proteins involved is transforming growth factor β-induced protein (TGFBIp), an extracellular matrix component that interacts with integrins but also produces corneal deposits when mutated. Human TGFBIp is a multi-domain 683-residue protein, which contains one CROPT domain and four FAS1 domains. Its structure spans ∼120 Å and reveals that vicinal domains FAS1-1/FAS1-2 and FAS1-3/FAS1-4 tightly interact in an equivalent manner. The FAS1 domains are sandwiches of two orthogonal four-stranded β sheets decorated with two three-helix insertions. The N-terminal FAS1 dimer forms a compact moiety with the structurally novel CROPT domain, which is a five-stranded all-β cysteine-knot solely found in TGFBIp and periostin. The overall TGFBIp architecture discloses regions for integrin binding and that most dystrophic mutations cluster at both molecule ends, within domains FAS1-1 and FAS1-4 | Versión del editor: | https://doi.org/10.1016/j.str.2017.09.001 | URI: | http://hdl.handle.net/10261/174536 | DOI: | 10.1016/j.str.2017.09.001 | ISSN: | 0969-2126 | E-ISSN: | 1878-4186 |
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