4v2d: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
==FLRT2 LRR domain==
==FLRT2 LRR domain==
<StructureSection load='4v2d' size='340' side='right' caption='[[4v2d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='4v2d' size='340' side='right' caption='[[4v2d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
Line 4: Line 5:
<table><tr><td colspan='2'>[[4v2d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V2D FirstGlance]. <br>
<table><tr><td colspan='2'>[[4v2d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V2D FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v2a|4v2a]], [[4v2b|4v2b]], [[4v2c|4v2c]], [[4v2e|4v2e]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v2a|4v2a]], [[4v2b|4v2b]], [[4v2c|4v2c]], [[4v2e|4v2e]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4v2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v2d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v2d RCSB], [http://www.ebi.ac.uk/pdbsum/4v2d PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4v2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v2d OCA], [http://pdbe.org/4v2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v2d RCSB], [http://www.ebi.ac.uk/pdbsum/4v2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v2d ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Line 14: Line 15:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4v2d" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 17:23, 27 April 2017

FLRT2 LRR domainFLRT2 LRR domain

Structural highlights

4v2d is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

FLRTs are broadly expressed proteins with the unique property of acting as homophilic cell adhesion molecules and as heterophilic repulsive ligands of Unc5/Netrin receptors. How these functions direct cell behavior and the molecular mechanisms involved remain largely unclear. Here we use X-ray crystallography to reveal the distinct structural bases for FLRT-mediated cell adhesion and repulsion in neurons. We apply this knowledge to elucidate FLRT functions during cortical development. We show that FLRTs regulate both the radial migration of pyramidal neurons, as well as their tangential spread. Mechanistically, radial migration is controlled by repulsive FLRT2-Unc5D interactions, while spatial organization in the tangential axis involves adhesive FLRT-FLRT interactions. Further, we show that the fundamental mechanisms of FLRT adhesion and repulsion are conserved between neurons and vascular endothelial cells. Our results reveal FLRTs as powerful guidance factors with structurally encoded repulsive and adhesive surfaces.

FLRT structure: balancing repulsion and cell adhesion in cortical and vascular development.,Seiradake E, del Toro D, Nagel D, Cop F, Hartl R, Ruff T, Seyit-Bremer G, Harlos K, Border EC, Acker-Palmer A, Jones EY, Klein R Neuron. 2014 Oct 22;84(2):370-85. doi: 10.1016/j.neuron.2014.10.008. Epub 2014, Oct 22. PMID:25374360[1]

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

References

  1. Seiradake E, del Toro D, Nagel D, Cop F, Hartl R, Ruff T, Seyit-Bremer G, Harlos K, Border EC, Acker-Palmer A, Jones EY, Klein R. FLRT structure: balancing repulsion and cell adhesion in cortical and vascular development. Neuron. 2014 Oct 22;84(2):370-85. doi: 10.1016/j.neuron.2014.10.008. Epub 2014, Oct 22. PMID:25374360 doi:http://dx.doi.org/10.1016/j.neuron.2014.10.008

4v2d, resolution 2.50Å

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