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Structural and Functional Implications of Human Transforming Growth Factor ß-Induced Protein, TGFBIp, in Corneal Dystrophies.
García-Castellanos, Raquel; Nielsen, Nadia Sukusu; Runager, Kasper; Thøgersen, Ida B; Lukassen, Marie V; Poulsen, Ebbe T; Goulas, Theodoros; Enghild, Jan J; Gomis-Rüth, F Xavier.
Afiliação
  • García-Castellanos R; Proteolysis Laboratory, Structural Biology Unit ("María-de-Maeztu" Unit of Excellence), Molecular Biology Institute of Barcelona (CSIC), Barcelona Science Park, c/Baldiri Reixac 15-21, 08028 Barcelona, Catalonia, Spain.
  • Nielsen NS; Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej, 10, 8000 Aarhus C, Denmark.
  • Runager K; Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej, 10, 8000 Aarhus C, Denmark.
  • Thøgersen IB; Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej, 10, 8000 Aarhus C, Denmark.
  • Lukassen MV; Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej, 10, 8000 Aarhus C, Denmark.
  • Poulsen ET; Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej, 10, 8000 Aarhus C, Denmark.
  • Goulas T; Proteolysis Laboratory, Structural Biology Unit ("María-de-Maeztu" Unit of Excellence), Molecular Biology Institute of Barcelona (CSIC), Barcelona Science Park, c/Baldiri Reixac 15-21, 08028 Barcelona, Catalonia, Spain.
  • Enghild JJ; Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej, 10, 8000 Aarhus C, Denmark.
  • Gomis-Rüth FX; Proteolysis Laboratory, Structural Biology Unit ("María-de-Maeztu" Unit of Excellence), Molecular Biology Institute of Barcelona (CSIC), Barcelona Science Park, c/Baldiri Reixac 15-21, 08028 Barcelona, Catalonia, Spain. Electronic address: xgrcri@ibmb.csic.es.
Structure ; 25(11): 1740-1750.e2, 2017 11 07.
Article em En | MEDLINE | ID: mdl-28988748
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 ß-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 ß 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-ß 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.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Integrinas / Proteínas da Matriz Extracelular / Fator de Crescimento Transformador beta / Agregados Proteicos / Mutação Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Integrinas / Proteínas da Matriz Extracelular / Fator de Crescimento Transformador beta / Agregados Proteicos / Mutação Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article