View source for 6cku


==Solution structure of the zebrafish granulin AaE==
<StructureSection load='6cku' size='340' side='right'caption='[[6cku]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6cku]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CKU FirstGlance]. <br>
</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=6cku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cku OCA], [https://pdbe.org/6cku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cku RCSB], [https://www.ebi.ac.uk/pdbsum/6cku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cku ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8QGN9_DANRE Q8QGN9_DANRE] 
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== Publication Abstract from PubMed ==
The ancient and pluripotent progranulins contain multiple repeats of a cysteine-rich sequence motif of approximately 60 amino acids, called the granulin/epithelin module (GEM) with a prototypic structure of four beta-hairpins zipped together by six inter-hairpin disulfide bonds. Prevalence of this disulfide-enforced structure is assessed here by an expression screening of 19 unique GEM sequences of the four progranulins in the zebrafish genome, progranulins 1, 2, A and B. While a majority of the expressed GEM peptides did not exhibit uniquely-folded conformations, module AaE from progranulin A and AbB from progranulin B were found to fold into the protopypic 4-hairpin structure along with disulfide formation. Module AaE has the most-rigid three-dimensional structure with all four beta-hairpins defined using high-resolution (H-(15) N) NMR spectroscopy, including 492 inter-proton nuclear Overhauser effects, 23 (3) J(HN,Halpha ) coupling constants, 22 hydrogen bonds as well as residual dipolar coupling constants. Three-dimensional structure of AaE and the partially-folded AbB re-iterate the conformational stability of the N-terminal stack of two beta-hairpins and varying degrees of structural flexibility for the C-terminal half of the 4-hairpin global fold of the GEM repeat. A cell-based assay demonstrated a functional activity for the zebrafish granulin AaE in promoting the survival of neuronal cells, similarly to what has been found for the corresponding granulin E module in human progranulin. Finally, this work highlights the remaining challenges in structure-activity studies of proteins containing the GEM repeats, due to the apparent prevalence of structural disorder in GEM motifs despite potentially a high density of intramolecular disulfide bonds. This article is protected by copyright. All rights reserved.

Structure Dissection of Zebrafish Progranulins Identifies a Well-Folded Granulin/Epithelin Module Protein with pro-Cell Survival Activities.,Wang P, Chitramuthu B, Bateman A, Bennett HPJ, Xu P, Ni F Protein Sci. 2018 May 7. doi: 10.1002/pro.3441. PMID:29732682<ref>PMID:29732682</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6cku" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Danio rerio]]
[[Category: Large Structures]]
[[Category: Ni F]]
[[Category: Wang P]]