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1iyf

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1iyf, 10 NMR models ()
Activity: Ubiquitin--protein ligase, with EC number 6.3.2.19
Domains: parkin_N
Resources: FirstGlance, OCA, PDBsum, RCSB, TOPSAN
Coordinates: save as pdb, mmCIF, xml



Solution structure of ubiquitin-like domain of human parkin

Publication Abstract from PubMed

Parkin, a product of the causative gene of autosomal-recessive juvenile parkinsonism (AR-JP), is a RING-type E3 ubiquitin ligase and has an amino-terminal ubiquitin-like (Ubl) domain. Although a single mutation that causes an Arg to Pro substitution at position 42 of the Ubl domain (the Arg 42 mutation) has been identified in AR-JP patients, the function of this domain is not clear. In this study, we determined the three-dimensional structure of the Ubl domain of parkin by NMR, in particular by extensive use of backbone (15)N-(1)H residual dipolar-coupling data. Inspection of chemical-shift-perturbation data showed that the parkin Ubl domain binds the Rpn10 subunit of 26S proteasomes via the region of parkin that includes position 42. Our findings suggest that the Arg 42 mutation induces a conformational change in the Rpn10-binding site of Ubl, resulting in impaired proteasomal binding of parkin, which could be the cause of AR-JP.

Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain., Sakata E, Yamaguchi Y, Kurimoto E, Kikuchi J, Yokoyama S, Yamada S, Kawahara H, Yokosawa H, Hattori N, Mizuno Y, Tanaka K, Kato K, EMBO Rep. 2003 Mar;4(3):301-6. PMID:12634850

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

About this Structure

1IYF is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

  • Sakata E, Yamaguchi Y, Kurimoto E, Kikuchi J, Yokoyama S, Yamada S, Kawahara H, Yokosawa H, Hattori N, Mizuno Y, Tanaka K, Kato K. Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain. EMBO Rep. 2003 Mar;4(3):301-6. PMID:12634850 doi:10.1038/sj.embor.embor764

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