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PDBsum entry 3gxe

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protein ligands Protein-protein interface(s) links
Cell adhesion PDB id
3gxe
Jmol
Contents
Protein chains
89 a.a. *
11 a.a. *
16 a.a. *
Ligands
NAG ×2
GOL
Waters ×44
* Residue conservation analysis
PDB id:
3gxe
Name: Cell adhesion
Title: Complex of a low affinity collagen site with the fibronectin domain pair
Structure: Fibronectin. Chain: b, a. Fragment: 8-9fni, unp residues 516-608. Synonym: fn, cold-insoluble globulin, cig, ugl-y1, ugl-y2, engineered: yes. Mutation: yes. Collagen alpha-1(i) chain. Chain: f. Fragment: coli.260, unp residues 254-275.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: fn. Expressed in: pichia pastoris. Expression_system_taxid: 4922. Synthetic: yes. Other_details: standard peptide synthesis. Other_details: standard peptide synthesis
Resolution:
2.60Å     R-factor:   0.223     R-free:   0.271
Authors: B.Sladek,I.D.Campbell,I.Vakonakis
Key ref: M.C.Erat et al. (2013). Structural analysis of collagen type I interactions with human fibronectin reveals a cooperative binding mode. J Biol Chem, 288, 17441-17450. PubMed id: 23653354 DOI: 10.1074/jbc.M113.469841
Date:
02-Apr-09     Release date:   07-Apr-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P02751  (FINC_HUMAN) -  Fibronectin
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2386 a.a.
89 a.a.*
Protein chain
Pfam   ArchSchema ?
P02452  (CO1A1_HUMAN) -  Collagen alpha-1(I) chain
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1464 a.a.
11 a.a.*
Protein chain
Pfam   ArchSchema ?
P02452  (CO1A1_HUMAN) -  Collagen alpha-1(I) chain
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1464 a.a.
16 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 

 

 
DOI no: 10.1074/jbc.M113.469841 J Biol Chem 288:17441-17450 (2013)
PubMed id: 23653354  
 
 
Structural analysis of collagen type I interactions with human fibronectin reveals a cooperative binding mode.
M.C.Erat, B.Sladek, I.D.Campbell, I.Vakonakis.
 
  ABSTRACT  
 
Despite its biological importance, the interaction between fibronectin (FN) and collagen, two abundant and crucial tissue components, has not been well characterized on a structural level. Here, we analyzed the four interactions formed between epitopes of collagen type I and the collagen-binding fragment (gelatin-binding domain (GBD)) of human FN using solution NMR, fluorescence, and small angle x-ray scattering methods. Collagen association with FN modules (8-9)FnI occurs through a conserved structural mechanism but exhibits a 400-fold disparity in affinity between collagen sites. This disparity is reduced in the full-length GBD, as (6)FnI(1-2)FnII(7)FnI binds a specific collagen epitope next to the weakest (8-9)FnI-binding site. The cooperative engagement of all GBD modules with collagen results in four broadly equipotent FN-collagen interaction sites. Collagen association stabilizes a distinct monomeric GBD conformation in solution, giving further evidence to the view that FN fragments form well defined functional and structural units.