5amo: Difference between revisions

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== Function ==

[[http://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.

== 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>

</div>

== References ==

__TOC__

</StructureSection>

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 == Function ==
 [[http://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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>