Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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DOI10.2210/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: 19251642
DOI: 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)
構造検証レポート
Validation report summary of 3ejh
検証レポート(詳細版)ダウンロードをダウンロード

252456

件を2026-04-22に公開中

PDB statisticsPDBj update infoContact PDBjnumon