¹H, ¹³C and ¹⁵N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment.
Fibrillins are large extracellular glycoproteins that form the principal component of microfibrils. These perform a vital structural function in the extracellular matrix of many tissues. Fibrillins have also been implicated in mediating a number of protein-protein interactions, some of which may be...
Main Authors: | , , , , , |
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Format: | Journal article |
Language: | English |
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2014
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author | Robertson, I Osuch, I Yadin, D Handford, P Jensen, SA Redfield, C |
author_facet | Robertson, I Osuch, I Yadin, D Handford, P Jensen, SA Redfield, C |
author_sort | Robertson, I |
collection | OXFORD |
description | Fibrillins are large extracellular glycoproteins that form the principal component of microfibrils. These perform a vital structural function in the extracellular matrix of many tissues. Fibrillins have also been implicated in mediating a number of protein-protein interactions, some of which may be significant in regulating growth factors such as transforming growth factor β. Here we present the backbone and side-chain (1)H, (13)C and (15)N assignments for a 19 kDa protein fragment derived from the N-terminus of human fibrillin-1, encompassing four domains in total. These domains include the second and third epidermal growth factor-like (EGF) domains, the first hybrid domain (hyb1), and the first calcium-binding EGF domain of fibrillin-1. This region of fibrillin-1 is of particular interest as the hyb1 domain has been suggested to play a role in microfibril assembly, as well as several other protein-protein interactions. |
first_indexed | 2024-03-06T21:29:02Z |
format | Journal article |
id | oxford-uuid:4409d621-d3cf-40d7-b49b-c0e2754c2ef1 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T21:29:02Z |
publishDate | 2014 |
record_format | dspace |
spelling | oxford-uuid:4409d621-d3cf-40d7-b49b-c0e2754c2ef12022-03-26T14:59:22Z¹H, ¹³C and ¹⁵N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4409d621-d3cf-40d7-b49b-c0e2754c2ef1EnglishSymplectic Elements at Oxford2014Robertson, IOsuch, IYadin, DHandford, PJensen, SARedfield, CFibrillins are large extracellular glycoproteins that form the principal component of microfibrils. These perform a vital structural function in the extracellular matrix of many tissues. Fibrillins have also been implicated in mediating a number of protein-protein interactions, some of which may be significant in regulating growth factors such as transforming growth factor β. Here we present the backbone and side-chain (1)H, (13)C and (15)N assignments for a 19 kDa protein fragment derived from the N-terminus of human fibrillin-1, encompassing four domains in total. These domains include the second and third epidermal growth factor-like (EGF) domains, the first hybrid domain (hyb1), and the first calcium-binding EGF domain of fibrillin-1. This region of fibrillin-1 is of particular interest as the hyb1 domain has been suggested to play a role in microfibril assembly, as well as several other protein-protein interactions. |
spellingShingle | Robertson, I Osuch, I Yadin, D Handford, P Jensen, SA Redfield, C ¹H, ¹³C and ¹⁵N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment. |
title | ¹H, ¹³C and ¹⁵N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment. |
title_full | ¹H, ¹³C and ¹⁵N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment. |
title_fullStr | ¹H, ¹³C and ¹⁵N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment. |
title_full_unstemmed | ¹H, ¹³C and ¹⁵N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment. |
title_short | ¹H, ¹³C and ¹⁵N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment. |
title_sort | ¹h ¹³c and ¹⁵n resonance assignments for the fibrillin 1 egf2 egf3 hybrid1 cbegf1 four domain fragment |
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