1w8a
From Proteopedia
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| - | [[Image:1w8a.gif|left|200px]]<br /><applet load="1w8a" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1w8a, resolution 2.8Å" /> | ||
| - | '''THIRD LRR DOMAIN OF DROSOPHILA SLIT'''<br /> | ||
| - | == | + | ==Third LRR domain of Drosophila Slit== |
| + | <StructureSection load='1w8a' size='340' side='right'caption='[[1w8a]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1w8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W8A FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w8a OCA], [https://pdbe.org/1w8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w8a RCSB], [https://www.ebi.ac.uk/pdbsum/1w8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w8a ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SLIT_DROME SLIT_DROME] A short-range repellent, controlling axon crossing of the midline and a long-range chemorepellent, controlling mesoderm migration and patterning away from the midline. May interact with extracellular matrix molecules. Repulsive ligand for the guidance receptor roundabout (robo) and prevents inappropriate midline crossing by Robo-expressing axons.<ref>PMID:2176636</ref> <ref>PMID:10102267</ref> <ref>PMID:3144436</ref> <ref>PMID:10102268</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w8/1w8a_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1w8a ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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<ref>PMID:15496984</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1w8a" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Clout | + | [[Category: Clout NJ]] |
| - | [[Category: Hohenester | + | [[Category: Hohenester E]] |
| - | [[Category: Howitt | + | [[Category: Howitt JA]] |
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Current revision
Third LRR domain of Drosophila Slit
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