Unknown

Dataset Information

0

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'.

SUBMITTER: Pickford AR 

PROVIDER: S-EPMC145459 | biostudies-literature | 2001 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Pickford A R AR   Smith S P SP   Staunton D D   Boyd J J   Campbell I D ID  

The EMBO journal 20010401 7


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 ne  ...[more]

Similar Datasets

2020-06-18 | GSE150411 | GEO
| S-EPMC1163603 | biostudies-other
| S-EPMC1162640 | biostudies-other
| S-EPMC3003407 | biostudies-literature
| S-EPMC4320333 | biostudies-literature
| S-EPMC2978626 | biostudies-literature
| S-EPMC3288308 | biostudies-literature
| S-EPMC6085428 | biostudies-literature
| S-EPMC9648752 | biostudies-literature
| S-EPMC1171236 | biostudies-other