Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a.

http://www.ncbi.nlm.nih.gov/pubmed/14557549

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.

Pubmed ID: 14557549 RIS Download

Mesh terms: Amino Acid Sequence | Binding Sites | Carrier Proteins | Cysteine Endopeptidases | DNA Repair | DNA Repair Enzymes | DNA-Binding Proteins | Humans | Magnetic Resonance Spectroscopy | Models, Molecular | Molecular Sequence Data | Multienzyme Complexes | Proteasome Endopeptidase Complex | Protein Binding | Protein Conformation | Protein Structure, Secondary | Protein Subunits

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.