Identification and structural analysis of type I collagen sites in complex with fibronectin fragments.
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, de...
Hlavní autoři: | Erat, M, Slatter, D, Lowe, E, Millard, C, Farndale, R, Campbell, I, Vakonakis, I |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
2009
|
Podobné jednotky
-
Structural analysis of collagen type I interactions with human fibronectin reveals a cooperative binding mode.
Autor: Erat, M, a další
Vydáno: (2013) -
Implications for collagen binding from the crystallographic structure of fibronectin 6FnI1-2FnII7FnI.
Autor: Erat, M, a další
Vydáno: (2010) -
Preparation of recombinant fibronectin fragments for functional and structural studies.
Autor: Staunton, D, a další
Vydáno: (2009) -
Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis.
Autor: Vakonakis, I, a další
Vydáno: (2007) -
The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules.
Autor: Atkin, K, a další
Vydáno: (2010)