5amo: Difference between revisions
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==Structure of a mouse Olfactomedin-1 disulfide-linked dimer of the Olfactomedin domain and part of the coiled coil== | |||
<StructureSection load='5amo' size='340' side='right'caption='[[5amo]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5amo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AMO 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]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5amo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5amo OCA], [https://pdbe.org/5amo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5amo RCSB], [https://www.ebi.ac.uk/pdbsum/5amo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5amo ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NOE1_MOUSE NOE1_MOUSE] May play an important role in regulating the production of neural crest cells by the neural tube. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Olfactomedin-1 (Olfm1; also known as noelin, pancortin) is a member of the olfactomedin domain-containing superfamily and a highly expressed neuronal glycoprotein important for nervous system development. It binds a number of secreted proteins and cell-surface bound receptors to induce cell signaling processes. Using a combined approach of X-ray crystallography, solution scattering, analytical ultracentrifugation and electron microscopy we determine that full-length Olfm1 forms disulfide-linked tetramers with a distinctive V-shaped architecture. The base of the ''V'' is formed by two disulfide-linked dimeric N-terminal domains. Each of the two V-legs consists of a parallel dimeric disulfide-linked coiled coil with at the tips a C-terminal beta-propeller dimer. This agrees with our crystal structure of a C-terminal coiled-coil segment and beta-propeller combination (Olfm1coil-Olf), which reveals a disulfide-linked dimeric arrangement with the beta-propeller top faces in an outward exposed orientation. Similar to its family member myocilin, Olfm1 is stabilized by calcium. The dimer-of-dimers architecture suggests a role for Olfm1 in clustering receptors to regulate signaling and informs on the conformation of several other olfactomedin domain family members. | |||
Olfactomedin-1 has a V-shaped disulfide-linked tetrameric structure.,Pronker MF, Bos TG, Sharp TH, Thies-Weesie DM, Janssen BJ J Biol Chem. 2015 Apr 21. pii: jbc.M115.653485. PMID:25903135<ref>PMID:25903135</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5amo" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Janssen | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Sharp | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Bos TGAA]] | |||
[[Category: Janssen BJC]] | |||
[[Category: Pronker MF]] | |||
[[Category: Sharp TH]] | |||
[[Category: Thies-Weesie DM]] | |||
Latest revision as of 11:13, 10 January 2024
Structure of a mouse Olfactomedin-1 disulfide-linked dimer of the Olfactomedin domain and part of the coiled coil
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