1tp4
From Proteopedia
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Solution structure of the XPC binding domain of hHR23A protein
Overview
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.
About this Structure
1TP4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the XPC binding domain of hHR23A reveals hydrophobic patches for protein interaction., Kamionka M, Feigon J, Protein Sci. 2004 Sep;13(9):2370-7. PMID:15322280
Page seeded by OCA on Mon Nov 12 19:26:39 2007
Categories: Homo sapiens | Single protein | Feigon, J. | Kamionka, M. | Dna repair | Ner | Rad23 | Xpc
