1TP4

Solution structure of the XPC binding domain of hHR23A protein

1TP4 の概要

• エントリーDOI: 10.2210/pdb1tp4/pdb
• 分子名称: UV excision repair protein RAD23 homolog A (1 entity in total)
• 機能のキーワード: dna repair, ner, xpc, rad23
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P54725
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10782.90

構造登録者

Kamionka, M.,Feigon, J. (登録日: 2004-06-15, 公開日: 2004-09-28, 最終更新日: 2024-05-22)

主引用文献

Kamionka, M.,Feigon, J.
Structure of the XPC binding domain of hHR23A reveals hydrophobic patches for protein interaction
Protein Sci., 13:2370-2377, 2004

PubMed 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.

PubMed: 15322280
DOI: 10.1110/ps.04824304

実験手法

SOLUTION NMR