7alt: Difference between revisions

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<StructureSection load='7alt' size='340' side='right'caption='[[7alt]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
<StructureSection load='7alt' size='340' side='right'caption='[[7alt]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7alt]] 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=7ALT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ALT FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ALT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ALT 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]] 2.03&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03&#8491;</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=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=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=7alt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7alt OCA], [https://pdbe.org/7alt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7alt RCSB], [https://www.ebi.ac.uk/pdbsum/7alt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7alt ProSAT]</span></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=7alt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7alt OCA], [https://pdbe.org/7alt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7alt RCSB], [https://www.ebi.ac.uk/pdbsum/7alt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7alt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SERR_DROME SERR_DROME] Acts as a ligand for Notch (N) receptor. Essential for proper ectodermal development. Serrate represents an element in a network of interacting molecules operating at the cell surface during the differentiation of certain tissues.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Accurate Notch signalling is critical for development and homeostasis. Fine-tuning of Notch-ligand interactions has substantial impact on signalling outputs. Recent structural studies have identified a conserved N-terminal C2 domain in human Notch ligands which confers phospholipid binding in vitro. Here, we show that Drosophila ligands Delta and Serrate adopt the same C2 domain structure with analogous variations in the loop regions, including the so-called beta1-2 loop that is involved in phospholipid binding. Mutations in the beta1-2 loop of the Delta C2 domain retain Notch binding but have impaired ability to interact with phospholipids in vitro. To investigate its role in vivo, we deleted five residues within the beta1-2 loop of endogenous Delta. Strikingly, this change compromises ligand function. The modified Delta enhances phenotypes produced by Delta loss-of-function alleles and suppresses that of Notch alleles. As the modified protein is present on the cell surface in normal amounts, these results argue that C2 domain phospholipid binding is necessary for robust signalling in vivo fine-tuning the balance of trans and cis ligand-receptor interactions.
The conserved C2 phospholipid-binding domain in Delta contributes to robust Notch signalling.,Martins T, Meng Y, Korona B, Suckling R, Johnson S, Handford PA, Lea SM, Bray SJ EMBO Rep. 2021 Oct 5;22(10):e52729. doi: 10.15252/embr.202152729. Epub 2021 Aug, 4. PMID:34347930<ref>PMID:34347930</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7alt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Johnson S]]
[[Category: Johnson S]]
[[Category: Lea SM]]
[[Category: Lea SM]]
[[Category: Suckling R]]
[[Category: Suckling R]]

Latest revision as of 11:34, 17 October 2024

Structure of Drosophila Serrate C2-DSL-EGF1-EGF2Structure of Drosophila Serrate C2-DSL-EGF1-EGF2

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.03Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

7alt, resolution 2.03Å

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