3EJH

Crystal Structure of the Fibronectin 8-9FnI Domain Pair in Complex with a Type-I Collagen Peptide

Summary for 3EJH

• Entry DOI: 10.2210/pdb3ejh/pdb
• Descriptor: Fibronectin, Collagen type-I a1 chain, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: fibronectin, collagen, protein complex, collagenase site, acute phase, cell adhesion, disease mutation, extracellular matrix, glycoprotein, heparin-binding, phosphoprotein, pyrrolidone carboxylic acid, secreted, sulfation
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 27129.78

Authors

Erat, M.C.,Lowe, E.D.,Campbell, I.D.,Vakonakis, I. (deposition date: 2008-09-18, release date: 2009-02-03, Last modification date: 2023-08-30)

Primary citation

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

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)