The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding.
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'.
Pickford
A R
AR
Department of Biochemistry and Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Smith
S P
SP
Staunton
D
D
Boyd
J
J
Campbell
I D
ID
D001665:Binding Sites; D018360:Crystallography, X-Ray; D005353:Fibronectins / Q000737:chemistry* / Q000378:metabolism; D005780:Gelatin / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012996:Solutions
D005353:Fibronectins; D010446:Peptide Fragments; D012996:Solutions; D005780:Gelatin