Structural insight into binding of Staphylococcus aureus to human fibronectin.
Staphylococcus aureus possesses cell-wall attached proteins that bind the human protein fibronectin (Fn). An intermodule interface between the 4F1 and 5F1 modules in the N-terminal domain of Fn is maintained on bacterial peptide binding but there is a small change in the intermodule orientation and...
| Հիմնական հեղինակներ: | , , , , , , |
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| Ձևաչափ: | Journal article |
| Լեզու: | English |
| Հրապարակվել է: |
2006
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| _version_ | 1826285499648573440 |
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| author | Pilka, E Werner, J Schwarz-Linek, U Pickford, A Meenan, N Campbell, I Potts, JR |
| author_facet | Pilka, E Werner, J Schwarz-Linek, U Pickford, A Meenan, N Campbell, I Potts, JR |
| author_sort | Pilka, E |
| collection | OXFORD |
| description | Staphylococcus aureus possesses cell-wall attached proteins that bind the human protein fibronectin (Fn). An intermodule interface between the 4F1 and 5F1 modules in the N-terminal domain of Fn is maintained on bacterial peptide binding but there is a small change in the intermodule orientation and alignment of beta-strands that are predicted to bind the peptide. The module pair is elongated, as in the unbound state. Combined with evidence that residues in both 4F1 and 5F1 are directly involved in peptide binding, this observation supports the hypothesis that, when bound to intact Fn, the bacterial protein adopts an unusual, highly extended conformation. |
| first_indexed | 2024-03-07T01:29:45Z |
| format | Journal article |
| id | oxford-uuid:933348c6-eca0-4fcb-bc19-c4a0bf0c7c25 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:29:45Z |
| publishDate | 2006 |
| record_format | dspace |
| spelling | oxford-uuid:933348c6-eca0-4fcb-bc19-c4a0bf0c7c252022-03-26T23:30:40ZStructural insight into binding of Staphylococcus aureus to human fibronectin.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:933348c6-eca0-4fcb-bc19-c4a0bf0c7c25EnglishSymplectic Elements at Oxford2006Pilka, EWerner, JSchwarz-Linek, UPickford, AMeenan, NCampbell, IPotts, JRStaphylococcus aureus possesses cell-wall attached proteins that bind the human protein fibronectin (Fn). An intermodule interface between the 4F1 and 5F1 modules in the N-terminal domain of Fn is maintained on bacterial peptide binding but there is a small change in the intermodule orientation and alignment of beta-strands that are predicted to bind the peptide. The module pair is elongated, as in the unbound state. Combined with evidence that residues in both 4F1 and 5F1 are directly involved in peptide binding, this observation supports the hypothesis that, when bound to intact Fn, the bacterial protein adopts an unusual, highly extended conformation. |
| spellingShingle | Pilka, E Werner, J Schwarz-Linek, U Pickford, A Meenan, N Campbell, I Potts, JR Structural insight into binding of Staphylococcus aureus to human fibronectin. |
| title | Structural insight into binding of Staphylococcus aureus to human fibronectin. |
| title_full | Structural insight into binding of Staphylococcus aureus to human fibronectin. |
| title_fullStr | Structural insight into binding of Staphylococcus aureus to human fibronectin. |
| title_full_unstemmed | Structural insight into binding of Staphylococcus aureus to human fibronectin. |
| title_short | Structural insight into binding of Staphylococcus aureus to human fibronectin. |
| title_sort | structural insight into binding of staphylococcus aureus to human fibronectin |
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