Title

Molecular modelling of the TSR domain of R-spondin 4

Authors

Leila Ayadi^1, *

Affiliation

¹Targets for Diagnosis and Therapy Centre of Biotechnology of Sfax, Sfax, Tunisia 3038

Email

leila.ayadi@ipeis.rnu.tn; * Corresponding author

Article Type

Web Server

Date

received August 28, 2008;  accepted September 13, 2008; published November 02, 2008

Abstract

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.

Keywords

TSR domain; R-spondin 4; heparin binding; molecular modelling

Citation

Ayadi, Bioinformation 3(3): 119-123 (2008)

Edited by

P. Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.