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(1)H, (13)C and (15)N 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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3955488/ https://www.ncbi.nlm.nih.gov/pubmed/23649688 http://dx.doi.org/10.1007/s12104-013-9481-7 |
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author | Robertson, Ian B. Osuch, Isabelle Yadin, David A. Handford, Penny A. Jensen, Sacha A. Redfield, Christina |
author_facet | Robertson, Ian B. Osuch, Isabelle Yadin, David A. Handford, Penny A. Jensen, Sacha A. Redfield, Christina |
author_sort | Robertson, Ian B. |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-3955488 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-39554882014-03-21 (1)H, (13)C and (15)N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment Robertson, Ian B. Osuch, Isabelle Yadin, David A. Handford, Penny A. Jensen, Sacha A. Redfield, Christina Biomol NMR Assign Article 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. Springer Netherlands 2013-05-07 2014 /pmc/articles/PMC3955488/ /pubmed/23649688 http://dx.doi.org/10.1007/s12104-013-9481-7 Text en © The Author(s) 2013 https://creativecommons.org/licenses/by/2.0/ Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. |
spellingShingle | Article Robertson, Ian B. Osuch, Isabelle Yadin, David A. Handford, Penny A. Jensen, Sacha A. Redfield, Christina (1)H, (13)C and (15)N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment |
title | (1)H, (13)C and (15)N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment |
title_full | (1)H, (13)C and (15)N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment |
title_fullStr | (1)H, (13)C and (15)N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment |
title_full_unstemmed | (1)H, (13)C and (15)N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment |
title_short | (1)H, (13)C and (15)N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment |
title_sort | (1)h, (13)c and (15)n resonance assignments for the fibrillin-1 egf2-egf3-hybrid1-cbegf1 four-domain fragment |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3955488/ https://www.ncbi.nlm.nih.gov/pubmed/23649688 http://dx.doi.org/10.1007/s12104-013-9481-7 |
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