Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites

Jan M. Gebauer, Florian Flachsenberg, Cordula Windler, Barbara Richer, Ulrich Baumann, Karsten Seeger*

*Korrespondierende/r Autor/-in für diese Arbeit

Abstract

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 KD of about 1 mm. These data show that vWFA2 has additional functions in the extracellular matrix besides interacting with type I collagen.

OriginalspracheEnglisch
ZeitschriftFEBS Open Bio
Jahrgang10
Ausgabenummer4
Seiten (von - bis)580-592
Seitenumfang13
DOIs
PublikationsstatusVeröffentlicht - 01.04.2020

Strategische Forschungsbereiche und Zentren

  • Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

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