5NV6
Structure of human transforming growth factor beta-induced protein (TGFBIp).
Summary for 5NV6
| Entry DOI | 10.2210/pdb5nv6/pdb |
| Descriptor | Transforming growth factor-beta-induced protein ig-h3, ACETATE ION (3 entities in total) |
| Functional Keywords | structural protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Secreted : Q15582 |
| Total number of polymer chains | 2 |
| Total formula weight | 149598.56 |
| Authors | Garcia-Castellanos, R.,Nielsen, S.N.,Runager, K.,Thogersen, B.I.,Goulas, T.,Enghild, J.J.,Gomis-Ruth, F.X. (deposition date: 2017-05-03, release date: 2017-08-09, Last modification date: 2024-11-13) |
| Primary citation | 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 Cited by 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: 28988748DOI: 10.1016/j.str.2017.09.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.93 Å) |
Structure validation
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