View source for 6qp9


==Drosophila Semaphorin 1a, extracellular domains 1-2==
<StructureSection load='6qp9' size='340' side='right'caption='[[6qp9]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qp9]] is a 2 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=6QP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QP9 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]] 3.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=6qp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qp9 OCA], [https://pdbe.org/6qp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qp9 RCSB], [https://www.ebi.ac.uk/pdbsum/6qp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qp9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SEM1A_DROME SEM1A_DROME] Involved in growth cone guidance through its role in axonal repulsion.<ref>PMID:15282266</ref> <ref>PMID:8269517</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Semaphorin ligands and their plexin receptors are one of the major cell guidance factors that trigger localised changes in the cytoskeleton. Binding of semaphorin homodimer to plexin brings two plexins in close proximity which is a prerequisite for plexin signalling. This model appears to be too simplistic to explain the complexity and functional versatility of these molecules. Here, we determine crystal structures for all members of Drosophila class 1 and 2 semaphorins. Unlike previously reported semaphorin structures, Sema1a, Sema2a and Sema2b show stabilisation of sema domain dimer formation via a disulfide bond. Unexpectedly, our structural and biophysical data show Sema1b is a monomer suggesting that semaphorin function may not be restricted to dimers. We demonstrate that semaphorins can form heterodimers with members of the same semaphorin class. This heterodimerization provides a potential mechanism for cross-talk between different plexins and co-receptors to allow fine-tuning of cell signalling.

Diversity of oligomerization in Drosophila semaphorins suggests a mechanism of functional fine-tuning.,Rozbesky D, Robinson RA, Jain V, Renner M, Malinauskas T, Harlos K, Siebold C, Jones EY Nat Commun. 2019 Aug 15;10(1):3691. doi: 10.1038/s41467-019-11683-y. PMID:31417095<ref>PMID:31417095</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qp9" style="background-color:#fffaf0;"></div>

==See Also==
*[[Semaphorin 3D structures|Semaphorin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Harlos K]]
[[Category: Jones EY]]
[[Category: Robinson RA]]
[[Category: Rozbesky D]]
[[Category: Siebold C]]