6fkn: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
Line 1: Line 1:


==Drosophila Plexin A in complex with Semaphorin 1b==
==Drosophila Plexin A in complex with Semaphorin 1b==
<StructureSection load='6fkn' size='340' side='right'caption='[[6fkn]]' scene=''>
<StructureSection load='6fkn' size='340' side='right'caption='[[6fkn]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FKN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6FKN FirstGlance]. <br>
<table><tr><td colspan='2'>[[6fkn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FKN FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6fkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fkn OCA], [http://pdbe.org/6fkn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fkn RCSB], [http://www.ebi.ac.uk/pdbsum/6fkn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fkn ProSAT]</span></td></tr>
</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PlexA, BcDNA:GM05237, D-Plex A, Dmel\CG11081, DPlexA, lincRNA.927, plex, plex A, Plex1, plexA, PlexA1, CG11081, Dmel_CG11081 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Sema1b, Sema-1b, Sema-1b-RB, semaphorin-like, CG6446, Dmel_CG6446 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=6fkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fkn OCA], [https://pdbe.org/6fkn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fkn RCSB], [https://www.ebi.ac.uk/pdbsum/6fkn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fkn ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Semaphorin ligands interact with plexin receptors to contribute to functions in the development of myriad tissues including neurite guidance and synaptic organisation within the nervous system. Cell-attached semaphorins interact in trans with plexins on opposing cells, but also in cis on the same cell. The interplay between trans and cis interactions is crucial for the regulated development of complex neural circuitry, but the underlying molecular mechanisms are uncharacterised. We have discovered a distinct mode of interaction through which the Drosophila semaphorin Sema1b and mouse Sema6A mediate binding in cis to their cognate plexin receptors. Our high-resolution structural, biophysical and in vitro analyses demonstrate that monomeric semaphorins can mediate a distinctive plexin binding mode. These findings suggest the interplay between monomeric vs dimeric states has a hereto unappreciated role in semaphorin biology, providing a mechanism by which Sema6s may balance cis and trans functionalities.
Structural basis of semaphorin-plexin cis interaction.,Rozbesky D, Verhagen MG, Karia D, Nagy GN, Alvarez L, Robinson RA, Harlos K, Padilla-Parra S, Pasterkamp RJ, Jones EY EMBO J. 2020 Jun 5:e102926. doi: 10.15252/embj.2019102926. PMID:32500924<ref>PMID:32500924</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fkn" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Plexin|Plexin]]
*[[Plexin|Plexin]]
*[[Semaphorin|Semaphorin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Drome]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Harlos K]]
[[Category: Harlos, K]]
[[Category: Jones EY]]
[[Category: Jones, E Y]]
[[Category: Rozbesky D]]
[[Category: Rozbesky, D]]
[[Category: Cis interaction]]
[[Category: Plexin]]
[[Category: Sema domain]]
[[Category: Semaphorin]]
[[Category: Signaling protein]]

Latest revision as of 13:23, 18 March 2021

Drosophila Plexin A in complex with Semaphorin 1bDrosophila Plexin A in complex with Semaphorin 1b

Structural highlights

6fkn is a 4 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:PlexA, BcDNA:GM05237, D-Plex A, Dmel\CG11081, DPlexA, lincRNA.927, plex, plex A, Plex1, plexA, PlexA1, CG11081, Dmel_CG11081 (DROME), Sema1b, Sema-1b, Sema-1b-RB, semaphorin-like, CG6446, Dmel_CG6446 (DROME)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Semaphorin ligands interact with plexin receptors to contribute to functions in the development of myriad tissues including neurite guidance and synaptic organisation within the nervous system. Cell-attached semaphorins interact in trans with plexins on opposing cells, but also in cis on the same cell. The interplay between trans and cis interactions is crucial for the regulated development of complex neural circuitry, but the underlying molecular mechanisms are uncharacterised. We have discovered a distinct mode of interaction through which the Drosophila semaphorin Sema1b and mouse Sema6A mediate binding in cis to their cognate plexin receptors. Our high-resolution structural, biophysical and in vitro analyses demonstrate that monomeric semaphorins can mediate a distinctive plexin binding mode. These findings suggest the interplay between monomeric vs dimeric states has a hereto unappreciated role in semaphorin biology, providing a mechanism by which Sema6s may balance cis and trans functionalities.

Structural basis of semaphorin-plexin cis interaction.,Rozbesky D, Verhagen MG, Karia D, Nagy GN, Alvarez L, Robinson RA, Harlos K, Padilla-Parra S, Pasterkamp RJ, Jones EY EMBO J. 2020 Jun 5:e102926. doi: 10.15252/embj.2019102926. PMID:32500924[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Rozbesky D, Verhagen MG, Karia D, Nagy GN, Alvarez L, Robinson RA, Harlos K, Padilla-Parra S, Pasterkamp RJ, Jones EY. Structural basis of semaphorin-plexin cis interaction. EMBO J. 2020 Jun 5:e102926. doi: 10.15252/embj.2019102926. PMID:32500924 doi:http://dx.doi.org/10.15252/embj.2019102926

6fkn, resolution 4.80Å

Drag the structure with the mouse to rotate

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

OCA