View source for 6x20


==PDZ domain from choanoflagellate GIPC (mbGIPC) bound to B1AR peptide==
<StructureSection load='6x20' size='340' side='right'caption='[[6x20]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6x20]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Monosiga_brevicollis Monosiga brevicollis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X20 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.402&#8491;</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=6x20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x20 OCA], [https://pdbe.org/6x20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x20 RCSB], [https://www.ebi.ac.uk/pdbsum/6x20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x20 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A9VCZ3_MONBE A9VCZ3_MONBE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Identification of the molecular networks that facilitated the evolution of multicellular animals from their unicellular ancestors is a fundamental problem in evolutionary cellular biology. Choanoflagellates are recognized as the closest extant nonmetazoan ancestors to animals. These unicellular eukaryotes can adopt a multicellular-like "rosette" state. Therefore, they are compelling models for the study of early multicellularity. Comparative studies revealed that a number of putative human orthologs are present in choanoflagellate genomes, suggesting that a subset of these genes were necessary for the emergence of multicellularity. However, previous work is largely based on sequence alignments alone, which does not confirm structural nor functional similarity. Here, we focus on the PDZ domain, a peptide-binding domain which plays critical roles in myriad cellular signaling networks and which underwent a gene family expansion in metazoan lineages. Using a customized sequence similarity search algorithm, we identified 178 PDZ domains in the Monosiga brevicollis proteome. This includes 11 previously unidentified sequences, which we analyzed using Rosetta and homology modeling. To assess conservation of protein structure, we solved high-resolution crystal structures of representative M. brevicollis PDZ domains that are homologous to human Dlg1 PDZ2, Dlg1 PDZ3, GIPC, and SHANK1 PDZ domains. To assess functional conservation, we calculated binding affinities for mbGIPC, mbSHANK1, mbSNX27, and mbDLG-3 PDZ domains from M. brevicollis. Overall, we find that peptide selectivity is generally conserved between these two disparate organisms, with one possible exception, mbDLG-3. Overall, our results provide novel insight into signaling pathways in a choanoflagellate model of primitive multicellularity.

Structural characterization and computational analysis of PDZ domains in Monosiga brevicollis.,Gao M, Mackley IGP, Mesbahi-Vasey S, Bamonte HA, Struyvenberg SA, Landolt L, Pederson NJ, Williams LI, Bahl CD, Brooks L 3rd, Amacher JF Protein Sci. 2020 Nov;29(11):2226-2244. doi: 10.1002/pro.3947. Epub 2020 Sep 25. PMID:32914530<ref>PMID:32914530</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6x20" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Monosiga brevicollis]]
[[Category: Amacher JF]]
[[Category: Gao M]]