3EJH
Crystal Structure of the Fibronectin 8-9FnI Domain Pair in Complex with a Type-I Collagen Peptide
3EJH の概要
| エントリーDOI | 10.2210/pdb3ejh/pdb |
| 分子名称 | Fibronectin, Collagen type-I a1 chain, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| 機能のキーワード | fibronectin, collagen, protein complex, collagenase site, acute phase, cell adhesion, disease mutation, extracellular matrix, glycoprotein, heparin-binding, phosphoprotein, pyrrolidone carboxylic acid, secreted, sulfation |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 27129.78 |
| 構造登録者 | Erat, M.C.,Lowe, E.D.,Campbell, I.D.,Vakonakis, I. (登録日: 2008-09-18, 公開日: 2009-02-03, 最終更新日: 2023-08-30) |
| 主引用文献 | Erat, M.C.,Slatter, D.A.,Lowe, E.D.,Millard, C.J.,Farndale, R.W.,Campbell, I.D.,Vakonakis, I. Identification and structural analysis of type I collagen sites in complex with fibronectin fragments. Proc.Natl.Acad.Sci.USA, 106:4195-4200, 2009 Cited by PubMed Abstract: Collagen and fibronectin are major components of vertebrate extracellular matrices. Their association and distribution control the development and properties of diverse tissues, but thus far no structural information has been available for the complex formed. Here, we report binding of a peptide, derived from the alpha(1) chain of type I collagen, to the gelatin-binding domain of human fibronectin and present the crystal structure of this peptide in complex with the (8-9)FnI domain pair. Both gelatin-binding domain subfragments, (6)FnI(1-2)FnII(7)FnI and (8-9)FnI, bind the same specific sequence on D-period 4 of collagen I alpha(1), adjacent to the MMP-1 cleavage site. (8-9)FnI also binds the equivalent sequence of the alpha(2) chain. The collagen peptide adopts an antiparallel beta-strand conformation, similar to structures of proteins from pathogenic bacteria bound to FnI domains. Analysis of the type I collagen sequence suggests multiple putative fibronectin-binding sites compatible with our structural model. We demonstrate, by kinetic unfolding experiments, that the triple-helical collagen state is destabilized by (8-9)FnI. This finding suggests a role for fibronectin in collagen proteolysis and tissue remodeling. PubMed: 19251642DOI: 10.1073/pnas.0812516106 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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