4qpy: Difference between revisions
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''' | ==Crystal structure of C1QL2== | ||
<StructureSection load='4qpy' size='340' side='right' caption='[[4qpy]], [[Resolution|resolution]] 2.38Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4qpy]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QPY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QPY FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qq2|4qq2]], [[4qqh|4qqh]], [[4qql|4qql]], [[4qqo|4qqo]], [[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=4qpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qpy RCSB], [http://www.ebi.ac.uk/pdbsum/4qpy PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/C1QL2_MOUSE C1QL2_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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
[[Category: Brunger, A | __TOC__ | ||
</StructureSection> | |||
[[Category: Brunger, A T]] | |||
[[Category: Ressl, S]] | [[Category: Ressl, S]] | ||
[[Category: Brain-specific angiogenesis inhibitor adhesion g-protein coupled receptor 3]] | |||
[[Category: Extracellular]] | |||
[[Category: Jelly roll fold]] | |||
[[Category: Protein binding]] | |||
