 |
PDBsum entry 3mql
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Cell adhesion
|
PDB id
|
|
|
|
3mql
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Implications for collagen binding from the crystallographic structure of fibronectin 6fni1-2fnii7fni.
|
|
|
Authors
|
|
M.C.Erat,
U.Schwarz-Linek,
A.R.Pickford,
R.W.Farndale,
I.D.Campbell,
I.Vakonakis.
|
|
|
Ref.
|
|
J Biol Chem, 2010,
285,
33764-33770.
|
|
|
PubMed id
|
|
|
|
|
Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
|
|
|
|
Abstract
|
|
|
Collagen and fibronectin (FN) are two abundant and essential components of the
vertebrate extracellular matrix; they interact directly with cellular receptors
and affect cell adhesion and migration. Past studies identified a FN fragment
comprising six modules, (6)FnI(1-2)FnII(7-9)FnI, and termed the gelatin binding
domain (GBD) as responsible for collagen interaction. Recently, we showed that
the GBD binds tightly to a specific site within type I collagen and determined
the structure of domains (8-9)FnI in complex with a peptide from that site.
Here, we present the crystallographic structure of domains
(6)FnI(1-2)FnII(7)FnI, which form a compact, globular unit through interdomain
interactions. Analysis of NMR titrations with single-stranded collagen peptides
reveals a dominant collagen interaction surface on domains (2)FnII and (7)FnI; a
similar surface appears involved in interactions with triple-helical peptides.
Models of the complete GBD, based on the new structure and the
(8-9)FnI·collagen complex show a continuous putative collagen binding surface.
We explore the implications of this model using long collagen peptides and
discuss our findings in the context of FN interactions with collagen fibrils.
|
|
|
|
|
|
|
