1E88

Solution structure of 6F11F22F2, a compact three-module fragment of the gelatin-binding domain of human fibronectin

Summary for 1E88

• Entry DOI: 10.2210/pdb1e88/pdb
• Related: 1E8B
• Descriptor: FIBRONECTIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: extracellular matrix glycoprotein, cell adhesion
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 18092.83

Authors

Pickford, A.R.,Smith, S.P.,Staunton, D.,Boyd, J.,Campbell, I.D. (deposition date: 2000-09-18, release date: 2000-10-09, Last modification date: 2024-10-16)

Primary citation

Pickford, A.R.,Smith, S.P.,Staunton, D.,Boyd, J.,Campbell, I.D.
The Hairpin Structure of the (6)F1(1)F2(2)F2 Fragment from Human Fibronectin Enhances Gelatin Binding
Embo J., 20:1519-1529, 2001

PubMed 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'.

PubMed: 11285216
DOI: 10.1093/EMBOJ/20.7.1519

Experimental method

SOLUTION NMR