4jde
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of PUD-1/PUD-2 heterodimer== | |
- | === | + | <StructureSection load='4jde' size='340' side='right' caption='[[4jde]], [[Resolution|resolution]] 1.90Å' scene=''> |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[4jde]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JDE FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">F15E11.13, Y19D10B.7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans]), F15E11.1, F15E11.14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans])</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=4jde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jde OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jde RCSB], [http://www.ebi.ac.uk/pdbsum/4jde PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | C. elegans PUD-1 and PUD-2, two proteins up-regulated in daf-2(loss-of-function) (PUD), are homologous 17-kD proteins with a large abundance increase in long-lived daf-2 mutant animals of reduced insulin signaling. In this study, we show that both PUD-1 and PUD-2 are abundantly expressed in the intestine and hypodermis, and form a heterodimer. We have solved their crystal structure to 1.9-A resolution and found that both proteins adopt similar beta-sandwich folds in the V-shaped dimer. In contrast, their homologs PUD-3, PUD-4, PUDL-1 and PUDL-2 are all monomeric proteins with distinct expression patterns in C. elegans. Thus, the PUD-1/PUD-2 heterodimer probably has a function distinct from their family members. Neither overexpression nor deletion of pud-1 and pud-2 affected the lifespan of WT or daf-2 mutant animals, suggesting that their induction in daf-2 worms does not contribute to longevity. Curiously, deletion of pud-1 and pud-2 was associated with a protective effect against paralysis induced by the amyloid beta-peptide (1-42), which further enhanced the protection conferred by daf-2(RNAi) against Abeta. | ||
- | + | Characterization of PUD-1 and PUD-2, two proteins up-regulated in a long-lived daf-2 mutant.,Ding YH, Du YG, Luo S, Li YX, Li TM, Yoshina S, Wang X, Klage K, Mitani S, Ye K, Dong MQ PLoS One. 2013 Jun 14;8(6):e67158. doi: 10.1371/journal.pone.0067158. Print 2013. PMID:23799143<ref>PMID:23799143</ref> | |
- | + | ||
- | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | + | </div> | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
- | [[Category: Luo, S | + | [[Category: Luo, S]] |
- | [[Category: Ye, K | + | [[Category: Ye, K]] |
[[Category: Beta sandwich]] | [[Category: Beta sandwich]] | ||
[[Category: Unknown function]] | [[Category: Unknown function]] |
Revision as of 06:38, 25 December 2014
Crystal structure of PUD-1/PUD-2 heterodimer
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