4plm: Difference between revisions
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<StructureSection load='4plm' size='340' side='right'caption='[[4plm]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='4plm' size='340' side='right'caption='[[4plm]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4plm]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4plm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PLM FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4plm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4plm OCA], [https://pdbe.org/4plm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4plm RCSB], [https://www.ebi.ac.uk/pdbsum/4plm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4plm ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/NET1_CHICK NET1_CHICK] Netrins control guidance of CNS commissural axons and peripheral motor axons. Promotes neurite outgrowth from commissural axons but acts as a chemorepellent for trochlear motor axons. These effects are mediated by distinct receptors. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Nikolov | [[Category: Nikolov DB]] | ||
[[Category: Xu | [[Category: Xu K]] | ||
Revision as of 10:17, 8 February 2023
Crystal Structure of Chicken Netrin-1 (LN-LE3)Crystal Structure of Chicken Netrin-1 (LN-LE3)
Structural highlights
FunctionNET1_CHICK Netrins control guidance of CNS commissural axons and peripheral motor axons. Promotes neurite outgrowth from commissural axons but acts as a chemorepellent for trochlear motor axons. These effects are mediated by distinct receptors. Publication Abstract from PubMedNetrins are secreted proteins that regulate axon guidance and neuronal migration. Deleted in colorectal cancer (DCC) is a well-established netrin-1 receptor mediating attractive responses. We provide evidence that its close relative neogenin is also a functional netrin-1 receptor that acts with DCC to mediate guidance in vivo. We determined the structures of a functional netrin-1 region, alone and in complexes with neogenin or DCC. Netrin-1 has a rigid elongated structure containing two receptor-binding sites at opposite ends through which it brings together receptor molecules. The ligand/receptor complexes reveal two distinct architectures: a 2:2 heterotetramer and a continuous ligand/receptor assembly. The differences result from different lengths of the linker connecting receptor domains fibronectin type III domain 4 (FN4) and FN5, which differs among DCC and neogenin splice variants, providing a basis for diverse signaling outcomes. Neural migration. Structures of netrin-1 bound to two receptors provide insight into its axon guidance mechanism.,Xu K, Wu Z, Renier N, Antipenko A, Tzvetkova-Robev D, Xu Y, Minchenko M, Nardi-Dei V, Rajashankar KR, Himanen J, Tessier-Lavigne M, Nikolov DB Science. 2014 Jun 13;344(6189):1275-9. doi: 10.1126/science.1255149. Epub 2014, May 29. PMID:24876346[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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