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 are...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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2001
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| _version_ | 1797070238460674048 |
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| author | Pickford, A Smith, S Staunton, D Boyd, J Campbell, I |
| author_facet | Pickford, A Smith, S Staunton, D Boyd, J Campbell, I |
| author_sort | Pickford, A |
| collection | OXFORD |
| description | 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'. |
| first_indexed | 2024-03-06T22:36:03Z |
| format | Journal article |
| id | oxford-uuid:59f1e8c8-b5a6-43dd-a7ef-245f1e8bf885 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:36:03Z |
| publishDate | 2001 |
| record_format | dspace |
| spelling | oxford-uuid:59f1e8c8-b5a6-43dd-a7ef-245f1e8bf8852022-03-26T17:12:39ZThe hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:59f1e8c8-b5a6-43dd-a7ef-245f1e8bf885EnglishSymplectic Elements at Oxford2001Pickford, ASmith, SStaunton, DBoyd, JCampbell, IThe 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'. |
| spellingShingle | Pickford, A Smith, S Staunton, D Boyd, J Campbell, I The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. |
| title | The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. |
| title_full | The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. |
| title_fullStr | The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. |
| title_full_unstemmed | The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. |
| title_short | The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. |
| title_sort | hairpin structure of the 6 f1 1 f2 2 f2 fragment from human fibronectin enhances gelatin binding |
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