PDBsum entry 3mql

Cell adhesion

PDB id

3mql

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Contents

			Protein chain

					209 a.a. *

			Ligands

					NAG


					MPD


					MRD ×2

			Waters ×2

* Residue conservation analysis

PDB id:

3mql

Links

Name:

Cell adhesion

Title:

Crystal structure of the fibronectin 6fni1-2fnii7fni fragment

Structure:

Fibronectin 1. Chain: a. Fragment: 6fni1-2fnii7fni, unp residues 305-515. Synonym: fibronectin 1, isoform cra_g. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: fn1, hcg_1813428. Expressed in: pichia pastoris. Expression_system_taxid: 4922. Other_details: genomic integration

Resolution:

3.00Å

R-factor:

0.203

R-free:

0.231

Authors:

M.C.Erat,I.D.Campbell,I.Vakonakis

Key ref:

M.C.Erat et al. (2010). Implications for collagen binding from the crystallographic structure of fibronectin 6FnI1-2FnII7FnI. J Biol Chem, 285, 33764-33770. PubMed id: 20739283

Date:

28-Apr-10

Release date:

25-Aug-10

PROCHECK

	Headers

	References

Protein chain

P02751 (FINC_HUMAN) - Fibronectin from Homo sapiens

Seq: Struc:

Seq: Struc:

Seq: Struc:

Seq: Struc:

Seq: Struc:					2477 a.a. 209 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)

	J Biol Chem 285:33764-33770 (2010)
PubMed id: 20739283

Implications for collagen binding from the crystallographic structure of fibronectin 6FnI1-2FnII7FnI.
M.C.Erat, U.Schwarz-Linek, A.R.Pickford, R.W.Farndale, I.D.Campbell, I.Vakonakis.

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.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20947497

L.M.Maurer, B.R.Tomasini-Johansson, W.Ma, D.S.Annis, N.L.Eickstaedt, M.G.Ensenberger, K.A.Satyshur, and D.F.Mosher (2010).
Extended binding site on fibronectin for the functional upstream domain of protein F1 of Streptococcus pyogenes.

J Biol Chem, 285, 41087-41099.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.