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

Journal article

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'.

Authors: Pickford, A; Smith, S; Staunton, D; Boyd, J; Campbell, I

• Publication status: Published
• Journal: EMBO journal
• Volume: 20
• Issue: 7
• Pages: 1519-1529
• Publication date: 2001-04-01
• DOI: 10.1093/emboj/20.7.1519
• EISSN: 1460-2075
• ISSN: 0261-4189
• Language: English
• Keywords: Gelatin; Humans; Crystallography, X-Ray; Models, Molecular; Binding Sites; Solutions; Protein Structure, Secondary; Fibronectins; Protein Structure, Tertiary; Peptide Fragments