6fkk: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 6fkk is ON HOLD
+==Drosophila Semaphorin 1b, extracellular domains 1-2==
+<StructureSection load='6fkk' size='340' side='right'caption='[[6fkk]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6fkk]] 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=6FKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FKK 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]] 2.78&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <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=6fkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fkk OCA], [https://pdbe.org/6fkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fkk RCSB], [https://www.ebi.ac.uk/pdbsum/6fkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fkk ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q7KK54_DROME Q7KK54_DROME]
+<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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6fkk" 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: Rozbesky D]]