5NV6

Structure of human transforming growth factor beta-induced protein (TGFBIp).

5NV6 の概要

• エントリーDOI: 10.2210/pdb5nv6/pdb
• 分子名称: Transforming growth factor-beta-induced protein ig-h3, ACETATE ION (3 entities in total)
• 機能のキーワード: structural protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Secreted : Q15582
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 149598.56

構造登録者

Garcia-Castellanos, R.,Nielsen, S.N.,Runager, K.,Thogersen, B.I.,Goulas, T.,Enghild, J.J.,Gomis-Ruth, F.X. (登録日: 2017-05-03, 公開日: 2017-08-09, 最終更新日: 2024-11-13)

主引用文献

Garcia-Castellanos, R.,Nielsen, N.S.,Runager, K.,Thgersen, I.B.,Lukassen, M.V.,Poulsen, E.T.,Goulas, T.,Enghild, J.J.,Gomis-Ruth, F.X.
Structural and Functional Implications of Human Transforming Growth Factor beta-Induced Protein, TGFBIp, in Corneal Dystrophies.
Structure, 25:1740-1750.e2, 2017

PubMed Abstract: 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.

PubMed: 28988748
DOI: 10.1016/j.str.2017.09.001

実験手法

X-RAY DIFFRACTION (2.93 Å)