UV excision repair protein: Difference between revisions

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== Function ==
== Function ==


'''UV 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.
'''UV 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 highlights ==
== Structural highlights ==

Revision as of 10:23, 17 March 2024


Function

UV 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 highlights

The protein contains a modular domain structure consisting of ubiquitin-like domain, ubiquitin-associated domain and XPC (xeroderma pigmentosum group C protein)-binding domain[1].


Structure of yeast Rad23 (green) complex with Rad4 (grey) (PDB entry 2qsf)

Drag the structure with the mouse to rotate

3D Structures of UV excision repair protein3D Structures of UV excision repair protein

Updated on 17-March-2024

ReferencesReferences

  1. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky