3HON

Crystal Structure of Human Collagen XVIII Trimerization Domain (cubic form)

3HON の概要

• エントリーDOI: 10.2210/pdb3hon/pdb
• 分子名称: Collagen alpha-1(XVIII) chain (1 entity in total)
• 機能のキーワード: collagen triple helix, trimerization domain, collagen xviii, multiplexin, alternative promoter usage, alternative splicing, cell adhesion, collagen, disulfide bond, extracellular matrix, glycoprotein, hydroxylation, metal-binding, polymorphism, secreted, zinc, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix . Non-collagenous domain 1: Secreted, extracellular space, extracellular matrix, basement membrane . Endostatin: Secreted : P39060
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6442.37

構造登録者

Boudko, S.P.,Bachinger, H.P. (登録日: 2009-06-02, 公開日: 2009-08-11, 最終更新日: 2024-02-21)

主引用文献

Boudko, S.P.,Sasaki, T.,Engel, J.,Lerch, T.F.,Nix, J.,Chapman, M.S.,Bachinger, H.P.
Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization Fold.
J.Mol.Biol., 392:787-802, 2009

PubMed Abstract: Collagens contain a unique triple-helical structure with a repeating sequence -G-X-Y-, where proline and hydroxyproline are major constituents in X and Y positions, respectively. Folding of the collagen triple helix requires trimerization domains. Once trimerized, collagen chains are correctly aligned and the folding of the triple helix proceeds in a zipper-like fashion. Here we report the isolation, characterization, and crystal structure of the trimerization domain of human type XVIII collagen, a member of the multiplexin family. This domain differs from all other known trimerization domains in other collagens and exhibits a high trimerization potential at picomolar concentrations. Strong chain association and high specificity of binding are needed for multiplexins, which are present at very low levels.

PubMed: 19631658
DOI: 10.1016/j.jmb.2009.07.057

実験手法

X-RAY DIFFRACTION (3 Å)