6cku: Difference between revisions

(4 intermediate revisions by the same user not shown)

Line 1:

~~'''Unreleased structure'''~~

The ~~entry 6cku~~ is ~~ON HOLD until sometime~~ in the ~~future~~

==Solution structure of the zebrafish granulin AaE==

== 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]

== 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.

~~Authors:~~ Wang, P., Ni, F.

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>

~~Description: Solution structure~~ of the ~~zebrafish granulin AaE~~

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

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: Ni, F]]

[[Category: Wang, P]]

== References ==

__TOC__

</StructureSection>

[[Category: Danio rerio]]

[[Category: Large Structures]]

[[Category: Ni F]]

[[Category: Wang P]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6cku is ON HOLD  until sometime in the future
+==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]
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Wang, P., Ni, F.
+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>
-Description: Solution structure of the zebrafish granulin AaE
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Ni, F]]
+<div class="pdbe-citations 6cku" style="background-color:#fffaf0;"></div>
-[[Category: Wang, P]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Danio rerio]]
+[[Category: Large Structures]]
+[[Category: Ni F]]
+[[Category: Wang P]]