4jde | pdb_00004jde
Crystal structure of PUD-1/PUD-2 heterodimer
Structural highlights
Publication Abstract from PubMedC. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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