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