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4qq2

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Crystal structure of C1QL1

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Retrieved from "http://52.214.119.220/wiki/index.php/4qq2"

Categories: Large Structures | Mus musculus | Brunger AT | Ressl S

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 ==Crystal structure of C1QL1==
-<StructureSection load='4qq2' size='340' side='right' caption='[[4qq2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='4qq2' size='340' side='right'caption='[[4qq2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4qq2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QQ2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4qq2]] is a 3 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=4QQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QQ2 FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.801&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qpy|4qpy]], [[4qqh|4qqh]], [[4qql|4qql]], [[4qqo|4qqo]], [[4qqp|4qqp]]</td></tr>
+<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>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C1ql1, C1qrf, Crf, Ctrp14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4qq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qq2 OCA], [https://pdbe.org/4qq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qq2 RCSB], [https://www.ebi.ac.uk/pdbsum/4qq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qq2 ProSAT]</span></td></tr>
-<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=4qq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qq2 OCA], [http://pdbe.org/4qq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qq2 RCSB], [http://www.ebi.ac.uk/pdbsum/4qq2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qq2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/C1QRF_MOUSE C1QRF_MOUSE]] May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses.<ref>PMID:21262840</ref>
+[https://www.uniprot.org/uniprot/C1QRF_MOUSE C1QRF_MOUSE] May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses.<ref>PMID:21262840</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4qq2" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Brunger, A T]]
+[[Category: Mus musculus]]
-[[Category: Ressl, S]]
+[[Category: Brunger AT]]
-[[Category: Brain-specific angiogenesis inhibitor g-protein coupled receptor]]
+[[Category: Ressl S]]
-[[Category: C1q]]
-[[Category: Extracellular]]
-[[Category: Jelly roll fold]]
-[[Category: Protein binding]]

4qq2

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Crystal structure of C1QL1

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