PDBsum entry 1e8b

Cell adhesion

PDB id: 1e8b

Contents

Protein chain

160 a.a. *

Ligands

NAG

* Residue conservation analysis

PDB id:

1e8b

Name:

Cell adhesion

Title:

Solution structure of 6f11f22f2, a compact three-module fragment of the gelatin-binding domain of human fibronectin

Structure:

Fibronectin. Chain: a. Fragment: 6f11f22f2, residues 305-464. Synonym: fn, cold-insoluble globulin, cig,. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: extracellular. Expressed in: pichia pastoris. Expression_system_taxid: 4922.

NMR struc:

1 models

Authors:

A.R.Pickford,S.P.Smith,D.Staunton,J.Boyd,I.D.Campbell

Key ref:

A.R.Pickford et al. (2001). The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. EMBO J, 20, 1519-1529. PubMed id: 11285216 DOI: 10.1093/emboj/20.7.1519

Date:

18-Sep-00 Release date: 15-Oct-00

Protein chain

P02751  (FINC_HUMAN) -  Fibronectin from Homo sapiens

Seq: 2477 a.a.

Struc: 160 a.a.

DOI no: 10.1093/emboj/20.7.1519

EMBO J 20:1519-1529 (2001)

PubMed id: 11285216

The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding.

A.R.Pickford, S.P.Smith, D.Staunton, J.Boyd, I.D.Campbell.

ABSTRACT

The solution structure of the (6)F1(1)F2(2)F2 fragment from the gelatin-binding region of fibronectin has been determined (Protein Data Bank entry codes 1e88 and 1e8b). The structure reveals an extensive hydrophobic interface between the non-contiguous (6)F1 and (2)F2 modules. The buried surface area between (6)F1 and (2)F2 ( approximately 870 A(2)) is the largest intermodule interface seen in fibronectin to date. The dissection of (6)F1(1)F2(2)F2 into the (6)F1(1)F2 pair and (2)F2 results in near-complete loss of gelatin-binding activity. The hairpin topology of (6)F1(1)F2(2)F2 may facilitate intramolecular contact between the matrix assembly regions flanking the gelatin-binding domain. This is the first high-resolution study to reveal a compact, globular arrangement of modules in fibronectin. This arrangement is not consistent with the view that fibronectin is simply a linear 'string of beads'.

Selected figure(s)

Figure 5.
Figure 5 Module reorganization upon dissection of 6F1^1F2^2F2. Ribbon diagrams of the minimized average structures of (A) 6F1^1F2^2F2 and (B) 6F1^1F2. The colour scheme for the secondary structure elements is as in Figure 3A -C. Side chains for which 6F1 -2F2 intermodule NOEs were observed (V10, Y12, S13, M16, L19 and L28 of 6F1, and L103, Q105, S111, N112, A114, L115, T145 and K153 for 2F2) are shown in cyan for 6F1 and purple for 2F2. Removal of the 2F2 module allows the side chain of Y68 (pink) in 1F2 to interact with L19 and L28 in 6F1.

Figure 6.
Figure 6 Global topologies of multimodule fibronectin fragments. Solvent-accessible surfaces have been superimposed over ribbon diagrams for the minimized average structure of 6F1^1F2^2F2, and the crystal structures of 7F3^8F3^9F3^10F3 (Leahy et al., 1996) and 12F3^13F3^14F3 (Sharma et al., 1999). The fragment structures are mapped onto the mosaic illustration of fibronectin, which has been folded to account for the hairpin structure of 6F1^1F2^2F2.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2001, 20, 1519-1529) copyright 2001.

Figures were selected by an automated process.