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pubmed-article:19238248pubmed:dateCreated2009-2-24lld:pubmed
pubmed-article:19238248pubmed:abstractTextR-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 cent 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.lld:pubmed
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pubmed-article:19238248pubmed:statusPubMed-not-MEDLINElld:pubmed
pubmed-article:19238248pubmed:issn0973-2063lld:pubmed
pubmed-article:19238248pubmed:authorpubmed-author:AyadiLeilaLlld:pubmed
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pubmed-article:19238248pubmed:volume3lld:pubmed
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pubmed-article:19238248pubmed:pagination119-23lld:pubmed
pubmed-article:19238248pubmed:year2008lld:pubmed
pubmed-article:19238248pubmed:articleTitleMolecular modelling of the TSR domain of R-spondin 4.lld:pubmed
pubmed-article:19238248pubmed:affiliationTargets for Diagnosis and Therapy Centre of Biotechnology of Sfax, Sfax, Tunisia 3038. leila.ayadi@ipeis.rnu.tnlld:pubmed
pubmed-article:19238248pubmed:publicationTypeJournal Articlelld:pubmed