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Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites
Type VII collagen is an extracellular matrix protein, which is important for skin stability; however, detailed information at the molecular level is scarce. The second vWFA (von Willebrand factor type A) domain of type VII collagen mediates important interactions, and immunization of mice induces sk...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7137805/ https://www.ncbi.nlm.nih.gov/pubmed/32031736 http://dx.doi.org/10.1002/2211-5463.12807 |
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author | Gebauer, Jan M. Flachsenberg, Florian Windler, Cordula Richer, Barbara Baumann, Ulrich Seeger, Karsten |
author_facet | Gebauer, Jan M. Flachsenberg, Florian Windler, Cordula Richer, Barbara Baumann, Ulrich Seeger, Karsten |
author_sort | Gebauer, Jan M. |
collection | PubMed |
description | Type VII collagen is an extracellular matrix protein, which is important for skin stability; however, detailed information at the molecular level is scarce. The second vWFA (von Willebrand factor type A) domain of type VII collagen mediates important interactions, and immunization of mice induces skin blistering in certain strains. To understand vWFA2 function and the pathophysiological mechanisms leading to skin blistering, we structurally characterized this domain by X‐ray crystallography and NMR spectroscopy. Cell adhesion assays identified two new interactions: one with β1 integrin via its RGD motif and one with laminin‐332. The latter interaction was confirmed by surface plasmon resonance with a K (D) of about 1 mm. These data show that vWFA2 has additional functions in the extracellular matrix besides interacting with type I collagen. |
format | Online Article Text |
id | pubmed-7137805 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71378052020-04-08 Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites Gebauer, Jan M. Flachsenberg, Florian Windler, Cordula Richer, Barbara Baumann, Ulrich Seeger, Karsten FEBS Open Bio Research Articles Type VII collagen is an extracellular matrix protein, which is important for skin stability; however, detailed information at the molecular level is scarce. The second vWFA (von Willebrand factor type A) domain of type VII collagen mediates important interactions, and immunization of mice induces skin blistering in certain strains. To understand vWFA2 function and the pathophysiological mechanisms leading to skin blistering, we structurally characterized this domain by X‐ray crystallography and NMR spectroscopy. Cell adhesion assays identified two new interactions: one with β1 integrin via its RGD motif and one with laminin‐332. The latter interaction was confirmed by surface plasmon resonance with a K (D) of about 1 mm. These data show that vWFA2 has additional functions in the extracellular matrix besides interacting with type I collagen. John Wiley and Sons Inc. 2020-03-14 /pmc/articles/PMC7137805/ /pubmed/32031736 http://dx.doi.org/10.1002/2211-5463.12807 Text en © 2020 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Gebauer, Jan M. Flachsenberg, Florian Windler, Cordula Richer, Barbara Baumann, Ulrich Seeger, Karsten Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites |
title | Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites |
title_full | Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites |
title_fullStr | Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites |
title_full_unstemmed | Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites |
title_short | Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites |
title_sort | structural and biophysical characterization of the type vii collagen vwfa2 subdomain leads to identification of two binding sites |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7137805/ https://www.ncbi.nlm.nih.gov/pubmed/32031736 http://dx.doi.org/10.1002/2211-5463.12807 |
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