5KF4
Crystal structure of FN3 domain (Residues P368-P466) of Human collagen XX
5KF4 の概要
エントリーDOI | 10.2210/pdb5kf4/pdb |
分子名称 | Collagen alpha-1(XX) chain (2 entities in total) |
機能のキーワード | fn3 domain, human collagen, contractile protein |
由来する生物種 | Homo sapiens (Human) |
細胞内の位置 | Secreted, extracellular space : Q9P218 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 41991.74 |
構造登録者 | |
主引用文献 | Zhao, J.,Ren, J.,Wang, N.,Cheng, Z.,Yang, R.,Lin, G.,Guo, Y.,Cai, D.,Xie, Y.,Zhao, X. Crystal structure of the second fibronectin type III (FN3) domain from human collagen alpha 1 type XX Acta Crystallogr F Struct Biol Commun, 73:695-700, 2017 Cited by PubMed Abstract: Collagen α1 type XX, which contains fibronectin type III (FN3) repeats involving six FN3 domains (referred to as the FN#1-FN#6 domains), is an unusual member of the fibril-associated collagens with interrupted triple helices (FACIT) subfamily of collagens. The results of standard protein BLAST suggest that the FN3 repeats might contribute to collagen α1 type XX acting as a cytokine receptor. To date, solution NMR structures of the FN#3, FN#4 and FN#6 domains have been determined. To obtain further structural evidence to understand the relationship between the structure and function of the FN3 repeats from collagen α1 type XX, the crystal structure of the FN#2 domain from human collagen α1 type XX (residues Pro386-Pro466; referred to as FN2-HCXX) was solved at 2.5 Å resolution. The crystal structure of FN2-HCXX shows an immunoglobulin-like fold containing a β-sandwich structure, which is formed by a three-stranded β-sheet (β1, β2 and β5) packed onto a four-stranded β-sheet (β3, β4, β6 and β7). Two consensus domains, tencon and fibcon, are structural analogues of FN2-HCXX. Fn8, an FN3 domain from human oncofoetal fibronectin, is the closest structural analogue of FN2-HCXX derived from a naturally occurring sequence. Based solely on the structural similarity of FN2-HCXX to other FN3 domains, the detailed functions of FN2-HCXX and the FN3 repeats in collagen α1 type XX cannot be identified. PubMed: 29199991DOI: 10.1107/S2053230X1701648X 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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