View source for 6grf


==Crystal structure of the tandem DUF26 ectodomain from the Arabidopsis thaliana cysteine-rich receptor-like protein PDLP8.==
<StructureSection load='6grf' size='340' side='right'caption='[[6grf]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6grf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GRF 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=6grf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6grf OCA], [https://pdbe.org/6grf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6grf RCSB], [https://www.ebi.ac.uk/pdbsum/6grf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6grf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PDLP8_ARATH PDLP8_ARATH] Modulates cell-to-cell trafficking.[UniProtKB:Q8GXV7]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Large protein families are a prominent feature of plant genomes and their size variation is a key element for adaptation. However, gene and genome duplications pose difficulties for functional characterization and translational research. Here we infer the evolutionary history of the DOMAIN OF UNKNOWN FUNCTION (DUF) 26-containing proteins. The DUF26 emerged in secreted proteins. Domain duplications and rearrangements led to the appearance of CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASES (CRKs) and PLASMODESMATA-LOCALIZED PROTEINS (PDLPs). The DUF26 is land plant-specific but structural analyses of PDLP ectodomains revealed strong similarity to fungal lectins and thus may constitute a group of plant carbohydrate-binding proteins. CRKs expanded through tandem duplications and preferential retention of duplicates following whole genome duplications, whereas PDLPs evolved according to the dosage balance hypothesis. We propose that new gene families mainly expand through small-scale duplications, while fractionation and genetic drift after whole genome multiplications drive families towards dosage balance.

Mechanistic insights into the evolution of DUF26-containing proteins in land plants.,Vaattovaara A, Brandt B, Rajaraman S, Safronov O, Veidenberg A, Luklova M, Kangasjarvi J, Loytynoja A, Hothorn M, Salojarvi J, Wrzaczek M Commun Biol. 2019 Feb 8;2:56. doi: 10.1038/s42003-019-0306-9. eCollection 2019. PMID:30775457<ref>PMID:30775457</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6grf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Brandt B]]
[[Category: Hothorn M]]