ArticleProtein science : a publication of the Protein Society2004
Structure of the XPC binding domain of hHR23A reveals hydrophobic patches for protein interaction.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 39 citations in OpenAlex.
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- AlphaFold predicted structure of the Hsp90-like domains of the neurodegeneration linked protein sacsin reveals key residues for ATPase activity.Frontiers in molecular biosciences · 2022Article
- Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A.Nature communications · 2021Article
- Novel frameshift mutation in theWorld journal of clinical cases · 2020Article
- SACS variants are a relevant cause of autosomal recessive hereditary motor and sensory neuropathy.Human genetics · 2018Article
- Structures of ubiquitin-like (Ubl) and Hsp90-like domains of sacsin provide insight into pathological mutations.The Journal of biological chemistry · 2018Article
- Binding of HIV-1 Vpr protein to the human homolog of the yeast DNA repair protein RAD23 (hHR23A) requires its xeroderma pigmentosum complementation group C binding (XPCB) domain as well as the ubiquitin-associated 2 (UBA2) domain.The Journal of biological chemistry · 2014Article
- Role of the ubiquitin ligase E6AP/UBE3A in controlling levels of the synaptic protein Arc.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Comparative analysis and functional mapping of SACS mutations reveal novel insights into sacsin repeated architecture.Human mutation · 2013Article
- Ubiquilin-1 is a molecular chaperone for the amyloid precursor protein.The Journal of biological chemistry · 2011Article
- DNA repair gets physical: mapping an XPA-binding site on ERCC1.DNA repair · 2008Review
- Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein.Biochemistry · 2006Article
- Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin.Protein science : a publication of the Protein Society · 2006Article
- Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Rad23 proteins are involved both in the ubiquitin-proteasome pathway and in nucleotide excision repair (NER), but the relationship between these two pathways is not yet understood. The two human homologs of Rad23, hHR23A and B, are functionally redundant in NER and interact with xeroderma pigmentosum complementation group C (XPC) protein. The XPC-hHR23 complex is responsible for the specific recognition of damaged DNA, which is an early step in NER. The interaction of the XPC binding domain (XPCB) of hHR23A/B with XPC protein has been shown to be important for its optimal function in NER. We have determined the solution structure of XPCB of hHR23A. The domain consists of five amphipathic helices and reveals hydrophobic patches on the otherwise highly hydrophilic domain surface. The patches are predicted to be involved in interaction with XPC. The XPCB domain has limited sequence homology with any proteins outside of the Rad23 family except for sacsin, a protein involved in spastic ataxia of Charlevoix-Saguenay, which contains a domain with 35% sequence identity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.