Cargando…

Molecular modelling of the TSR domain of R-spondin 4

R-spondin 4 is a secreted protein mainly associated with embryonic nail development. R-spondins have been recently identified as heparin-binding proteins with high affinity. Proteoglycan binding has been associated with both the TSR and the C terminal basic amino acid rich domains. In this paper, mo...

Descripción completa

Detalles Bibliográficos
Autor principal: Ayadi, Leila
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics Publishing Group 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2639684/
https://www.ncbi.nlm.nih.gov/pubmed/19238248
_version_ 1782164493052149760
author Ayadi, Leila
author_facet Ayadi, Leila
author_sort Ayadi, Leila
collection PubMed
description R-spondin 4 is a secreted protein mainly associated with embryonic nail development. R-spondins have been recently identified as heparin-binding proteins with high affinity. Proteoglycan binding has been associated with both the TSR and the C terminal basic amino acid rich domains. In this paper, molecular modelling techniques were used to construct the model of R-spondin 4 TSR domain based on the structure of the F-spondin TSR domain 4 (30-40¢ sequence identity). Beside a positively charged surface in the TSR domain, presence of the basic amino acid rich domain which could forms a continuous heparin binding surface may explain the high affinity of R-spondins for heparin. Our results provide a framework for understanding the possible regulatory role of heparin in R-spondins signalling.
format Text
id pubmed-2639684
institution National Center for Biotechnology Information
language English
publishDate 2008
publisher Biomedical Informatics Publishing Group
record_format MEDLINE/PubMed
spelling pubmed-26396842009-02-23 Molecular modelling of the TSR domain of R-spondin 4 Ayadi, Leila Bioinformation Hypothesis R-spondin 4 is a secreted protein mainly associated with embryonic nail development. R-spondins have been recently identified as heparin-binding proteins with high affinity. Proteoglycan binding has been associated with both the TSR and the C terminal basic amino acid rich domains. In this paper, molecular modelling techniques were used to construct the model of R-spondin 4 TSR domain based on the structure of the F-spondin TSR domain 4 (30-40¢ sequence identity). Beside a positively charged surface in the TSR domain, presence of the basic amino acid rich domain which could forms a continuous heparin binding surface may explain the high affinity of R-spondins for heparin. Our results provide a framework for understanding the possible regulatory role of heparin in R-spondins signalling. Biomedical Informatics Publishing Group 2008-11-02 /pmc/articles/PMC2639684/ /pubmed/19238248 Text en © 2007 Biomedical Informatics Publishing Group This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Ayadi, Leila
Molecular modelling of the TSR domain of R-spondin 4
title Molecular modelling of the TSR domain of R-spondin 4
title_full Molecular modelling of the TSR domain of R-spondin 4
title_fullStr Molecular modelling of the TSR domain of R-spondin 4
title_full_unstemmed Molecular modelling of the TSR domain of R-spondin 4
title_short Molecular modelling of the TSR domain of R-spondin 4
title_sort molecular modelling of the tsr domain of r-spondin 4
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2639684/
https://www.ncbi.nlm.nih.gov/pubmed/19238248
work_keys_str_mv AT ayadileila molecularmodellingofthetsrdomainofrspondin4