Backbone ¹H, ¹³C and ¹⁵N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues.
Latent TGFβ binding protein 1 (LTBP1) is a large extracellular protein that has been shown to bind covalently to the propeptide of TGFβ cytokines and form a large latent complex, which is then incapable of binding TGFβ receptors. LTBP1 has also been demonstrated to interact with a number of insolubl...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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2014
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| _version_ | 1797054250500489216 |
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| author | Robertson, I Handford, P Redfield, C |
| author_facet | Robertson, I Handford, P Redfield, C |
| author_sort | Robertson, I |
| collection | OXFORD |
| description | Latent TGFβ binding protein 1 (LTBP1) is a large extracellular protein that has been shown to bind covalently to the propeptide of TGFβ cytokines and form a large latent complex, which is then incapable of binding TGFβ receptors. LTBP1 has also been demonstrated to interact with a number of insoluble extracellular matrix components, such as fibrillin, which may play a role in TGFβ regulation. Here we present the backbone (1)H, (13)C and (15)N assignments for two EGF domains of human LTBP1, and flanking regions, together forming a 12 kDa protein fragment at the C-terminus of LTBP1. This region is of particular interest as it is postulated to be involved in interactions with fibrillin microfibrils. |
| first_indexed | 2024-03-06T18:54:33Z |
| format | Journal article |
| id | oxford-uuid:115cd8c1-d422-45f6-bc01-22aff6dfa6ed |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:54:33Z |
| publishDate | 2014 |
| record_format | dspace |
| spelling | oxford-uuid:115cd8c1-d422-45f6-bc01-22aff6dfa6ed2022-03-26T10:02:00ZBackbone ¹H, ¹³C and ¹⁵N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:115cd8c1-d422-45f6-bc01-22aff6dfa6edEnglishSymplectic Elements at Oxford2014Robertson, IHandford, PRedfield, CLatent TGFβ binding protein 1 (LTBP1) is a large extracellular protein that has been shown to bind covalently to the propeptide of TGFβ cytokines and form a large latent complex, which is then incapable of binding TGFβ receptors. LTBP1 has also been demonstrated to interact with a number of insoluble extracellular matrix components, such as fibrillin, which may play a role in TGFβ regulation. Here we present the backbone (1)H, (13)C and (15)N assignments for two EGF domains of human LTBP1, and flanking regions, together forming a 12 kDa protein fragment at the C-terminus of LTBP1. This region is of particular interest as it is postulated to be involved in interactions with fibrillin microfibrils. |
| spellingShingle | Robertson, I Handford, P Redfield, C Backbone ¹H, ¹³C and ¹⁵N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues. |
| title | Backbone ¹H, ¹³C and ¹⁵N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues. |
| title_full | Backbone ¹H, ¹³C and ¹⁵N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues. |
| title_fullStr | Backbone ¹H, ¹³C and ¹⁵N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues. |
| title_full_unstemmed | Backbone ¹H, ¹³C and ¹⁵N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues. |
| title_short | Backbone ¹H, ¹³C and ¹⁵N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues. |
| title_sort | backbone ¹h ¹³c and ¹⁵n resonance assignment of the c terminal egf cbegf pair of ltbp1 and flanking residues |
| work_keys_str_mv | AT robertsoni backbone1h13cand15nresonanceassignmentofthecterminalegfcbegfpairofltbp1andflankingresidues AT handfordp backbone1h13cand15nresonanceassignmentofthecterminalegfcbegfpairofltbp1andflankingresidues AT redfieldc backbone1h13cand15nresonanceassignmentofthecterminalegfcbegfpairofltbp1andflankingresidues |