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4qqh

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==Crystal structure of C1QL3 in space group H32==
==Crystal structure of C1QL3 in space group H32==
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<StructureSection load='4qqh' size='340' side='right' caption='[[4qqh]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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<StructureSection load='4qqh' size='340' side='right'caption='[[4qqh]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qqh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QQH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QQH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4qqh]] is a 1 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=4QQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QQH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qpy|4qpy]], [[4qq2|4qq2]], [[4qql|4qql]], [[4qqo|4qqo]], [[4qqp|4qqp]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
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<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=4qqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qqh RCSB], [http://www.ebi.ac.uk/pdbsum/4qqh PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqh OCA], [https://pdbe.org/4qqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qqh RCSB], [https://www.ebi.ac.uk/pdbsum/4qqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qqh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/C1QL3_MOUSE C1QL3_MOUSE]] May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses. Plays a role in glucose homeostasis. Via AMPK signaling pathway, stimulates glucose uptake in adipocytes, myotubes and hepatocytes and enhances insulin-stimulated glucose uptake. In a hepatoma cell line, reduces the expression of gluconeogenic enzymes G6PC and PCK1 and hence decreases de novo glucose production.<ref>PMID:21262840</ref> <ref>PMID:21378161</ref>
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[https://www.uniprot.org/uniprot/C1QL3_MOUSE C1QL3_MOUSE] May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses. Plays a role in glucose homeostasis. Via AMPK signaling pathway, stimulates glucose uptake in adipocytes, myotubes and hepatocytes and enhances insulin-stimulated glucose uptake. In a hepatoma cell line, reduces the expression of gluconeogenic enzymes G6PC and PCK1 and hence decreases de novo glucose production.<ref>PMID:21262840</ref> <ref>PMID:21378161</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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C1q-like (C1QL) -1, -2, and -3 proteins are encoded by homologous genes that are highly expressed in brain. C1QLs bind to brain-specific angiogenesis inhibitor 3 (BAI3), an adhesion-type G-protein coupled receptor that may regulate dendritic morphology by organizing actin filaments. To begin to understand the function of C1QLs, we determined high-resolution crystal structures of the globular C1q-domains of C1QL1, C1QL2, and C1QL3. Each structure is a trimer, with each protomer forming a jelly-roll fold consisting of 10 beta strands. Moreover, C1QL trimers may assemble into higher-order oligomers similar to adiponectin and contain four Ca(2+)-binding sites along the trimeric symmetry axis, as well as additional surface Ca(2+)-binding sites. Mutation of Ca(2+)-coordinating residues along the trimeric symmetry axis lowered the Ca(2+)-binding affinity and protein stability. Our results reveal unique structural features of C1QLs among C1q/TNF superfamily proteins that may be associated with their specific brain functions.
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Structures of C1q-like Proteins Reveal Unique Features among the C1q/TNF Superfamily.,Ressl S, Vu BK, Vivona S, Martinelli DC, Sudhof TC, Brunger AT Structure. 2015 Apr 7;23(4):688-99. doi: 10.1016/j.str.2015.01.019. Epub 2015 Mar, 5. PMID:25752542<ref>PMID:25752542</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Brunger, A T]]
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[[Category: Large Structures]]
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[[Category: Ressl, S]]
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[[Category: Mus musculus]]
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[[Category: Brain-specific angiogenesis inhibitor g-protein coupled receptor 3]]
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[[Category: Brunger AT]]
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[[Category: C1q]]
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[[Category: Ressl S]]
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[[Category: Extracellular]]
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[[Category: Jelly roll fold]]
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[[Category: Protein binding]]
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Current revision

Crystal structure of C1QL3 in space group H32

PDB ID 4qqh

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