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4qqo

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Revision as of 18:32, 1 February 2017

Crystal structure of C1QL3 mutant D205A

Structural highlights

4qqo is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4qpy, 4qq2, 4qqh, 4qql, 4qqp
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bolliger MF, Martinelli DC, Sudhof TC. The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins. Proc Natl Acad Sci U S A. 2011 Feb 8;108(6):2534-9. doi: 10.1073/pnas.1019577108., Epub 2011 Jan 24. PMID:21262840 doi:http://dx.doi.org/10.1073/pnas.1019577108
↑ Wei Z, Peterson JM, Wong GW. Metabolic regulation by C1q/TNF-related protein-13 (CTRP13): activation OF AMP-activated protein kinase and suppression of fatty acid-induced JNK signaling. J Biol Chem. 2011 May 6;286(18):15652-65. doi: 10.1074/jbc.M110.201087. Epub 2011, Mar 4. PMID:21378161 doi:http://dx.doi.org/10.1074/jbc.M110.201087
↑ Ressl S, Vu BK, Vivona S, Martinelli DC, Sudhof TC, Brunger AT. Structures of C1q-like Proteins Reveal Unique Features among the C1q/TNF Superfamily. Structure. 2015 Apr 7;23(4):688-99. doi: 10.1016/j.str.2015.01.019. Epub 2015 Mar, 5. PMID:25752542 doi:http://dx.doi.org/10.1016/j.str.2015.01.019

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of C1QL3 mutant D205A==
 <StructureSection load='4qqo' size='340' side='right' caption='[[4qqo]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qpy|4qpy]], [[4qq2|4qq2]], [[4qqh|4qqh]], [[4qql|4qql]], [[4qqp|4qqp]]</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=4qqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qqo RCSB], [http://www.ebi.ac.uk/pdbsum/4qqo PDBsum]</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=4qqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqo OCA], [http://pdbe.org/4qqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qqo RCSB], [http://www.ebi.ac.uk/pdbsum/4qqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qqo ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4qqo" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4qqo

From Proteopedia

Revision as of 18:32, 1 February 2017

Crystal structure of C1QL3 mutant D205A

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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