1w8a
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(New page: 200px<br /><applet load="1w8a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w8a, resolution 2.8Å" /> '''THIRD LRR DOMAIN OF D...)
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Revision as of 03:08, 21 November 2007
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THIRD LRR DOMAIN OF DROSOPHILA SLIT
Overview
Recognition of the large secreted protein Slit by receptors of the Robo, family provides fundamental signals in axon guidance and other, developmental processes. In Drosophila, Slit-Robo signalling regulates, midline crossing and the lateral position of longitudinal axon tracts. We, report the functional dissection of Drosophila Slit, using structure, analysis, site-directed mutagenesis and in vitro assays. The N-terminal, region of Slit consists of a tandem array of four independently folded, leucine-rich repeat (LRR) domains, connected by disulphide-tethered, linkers. All three Drosophila Robos were found to compete for a single, highly conserved site on the concave face of the second LRR domain of, Slit. We also found that this domain is sufficient for biological activity, in a chemotaxis assay. Other Slit activities may require Slit dimerisation, mediated by the fourth LRR domain. Our results show that a small portion, of Slit is able to induce Robo signalling and indicate that the distinct, functions of Drosophila Robos are encoded in their divergent cytosolic, domains.
About this Structure
1W8A is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Binding site for Robo receptors revealed by dissection of the leucine-rich repeat region of Slit., Howitt JA, Clout NJ, Hohenester E, EMBO J. 2004 Nov 10;23(22):4406-12. Epub 2004 Oct 21. PMID:15496984
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