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| {{STRUCTURE_1w8a| PDB=1w8a | SCENE= }} | | {{STRUCTURE_1w8a| PDB=1w8a | SCENE= }} |
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| '''THIRD LRR DOMAIN OF DROSOPHILA SLIT'''
| | ===THIRD LRR DOMAIN OF DROSOPHILA SLIT=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15496984}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15496984 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15496984}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Secreted protein]] | | [[Category: Secreted protein]] |
| [[Category: Signal protein]] | | [[Category: Signal protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:17:46 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:45:50 2008'' |
