1oqy
Structure of the DNA repair protein hHR23a
|
OverviewOverview
The Rad23 family of proteins, including the human homologs hHR23a and, hHR23b, stimulates nucleotide excision repair and has been shown to, provide a novel link between proteasome-mediated protein degradation and, DNA repair. In this work, we illustrate how the proteasomal subunit S5a, regulates hHR23a protein structure. By using NMR spectroscopy, we have, elucidated the structure and dynamic properties of the 40-kDa hHR23a, protein and show it to contain four structured domains connected by, flexible linker regions. In addition, we reveal that these domains, interact in an intramolecular fashion, and by using residual dipolar, coupling data in combination with chemical shift perturbation analysis, we, present the hHR23a structure. By itself, hHR23a adopts a closed, conformation defined by the interaction of an N-terminal ubiquitin-like, domain with two ubiquitin-associated domains. Interestingly, binding of, the proteasomal subunit S5a disrupts the hHR23a interdomain interactions, and thereby causes it to adopt an opened conformation.
About this StructureAbout this Structure
1OQY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a., Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM, Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12694-9. Epub 2003 Oct 13. PMID:14557549
Page seeded by OCA on Mon Nov 12 18:35:43 2007