UV excision repair protein: Difference between revisions
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**[[2nbu]] – yRad23 UBL domain – yeast - NMR<br /> | **[[2nbu]] – yRad23 UBL domain – yeast - NMR<br /> | ||
**[[2qsf]] – yRad23 XPC-binding domain + Rad4 <br /> | **[[2qsf]] – yRad23 XPC-binding domain + Rad4 <br /> | ||
**[[2qsg]], [[2qsh]], [[4yir]], [[6cfi]] – yRad23 XPC-binding domain + Rad4 + DNA <br /> | **[[2qsg]], [[2qsh]], [[4yir]], [[6cfi]], [[6ubf]], [[6uin]] – yRad23 XPC-binding domain + Rad4 + DNA <br /> | ||
**[[1x3w]], [[3esw]] – yRad23 XPC-binding domain + peptide:N-glycanase<br /> | **[[1x3w]], [[3esw]] – yRad23 XPC-binding domain + peptide:N-glycanase<br /> | ||
**[[1x3z]] – yRad23 XPC-binding domain + peptide:N-glycanase + peptide<br /> | **[[1x3z]] – yRad23 XPC-binding domain + peptide:N-glycanase + peptide<br /> | ||
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**[[1p98]], [[2wyq]] – hHR23A UBA domain - NMR<br /> | **[[1p98]], [[2wyq]] – hHR23A UBA domain - NMR<br /> | ||
**[[1p9d]] – hHR23A UBA domain + S5a - NMR<br /> | **[[1p9d]] – hHR23A UBA domain + S5a - NMR<br /> | ||
**[[1tp4]] – hHR23A XPC-binding domain - NMR<br /> | **[[1tp4]] – hHR23A XPC-binding domain - NMR<br /> | ||
Revision as of 10:24, 10 January 2021
FunctionUV excision repair protein (Rad23) is a yeast protein involved in nucleotide excision repair. The human homologs are hHR23A and hHR23B. hHR23A plays a role in translocating polyubiquitinated proteins to the proteasome. Structural highlightsThe protein contains a modular domain structure consisting of ubiquitin-like domain, ubiquitin-associated domain and XPC(xeroderma pigmentosum group C protein)-binding domain[1].
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3D Structures of UV excision repair protein3D Structures of UV excision repair protein
Updated on 10-January-2021
ReferencesReferences
- ↑ Chen YW, Tajima T, Agrawal S. The crystal structure of the ubiquitin-like (UbL) domain of human homologue A of Rad23 (hHR23A) protein. Protein Eng Des Sel. 2010 Nov 3. PMID:21047872 doi:10.1093/protein/gzq084