1PVE

Solution structure of XPC binding domain of hHR23B

Summary for 1PVE

• Entry DOI: 10.2210/pdb1pve/pdb
• NMR Information: BMRB: 5868
• Descriptor: UV excision repair protein RAD23 homolog B (1 entity in total)
• Functional Keywords: hhr23b, xpc binding domain, nmr solution structure, nucleotide excision repair, chaps, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P54727
• Total number of polymer chains: 1
• Total formula weight: 8145.15

Authors

Kim, B.,Ryu, K.-S.,Kim, H.J.,Choi, B.-S. (deposition date: 2003-06-27, release date: 2004-08-10, Last modification date: 2024-05-29)

Primary citation

Kim, B.,Ryu, K.S.,Kim, H.J.,Cho, S.J.,Choi, B.S.
Solution structure and backbone dynamics of the XPC-binding domain of the human DNA repair protein hHR23B.
Febs J., 272:2467-2476, 2005

PubMed Abstract: Human cells contain two homologs of the yeast RAD23 protein, hHR23A and hHR23B, which participate in the DNA repair process. hHR23B houses a domain (residues 277-332, called XPCB) that binds specifically and directly to the xeroderma pigmentosum group C protein (XPC) to initiate nucleotide excision repair (NER). This domain shares sequence homology with a heat shock chaperonin-binding motif that is also found in the stress-inducible yeast phosphoprotein STI1. We determined the solution structure of a protein fragment containing amino acids 275-342 of hHR23B (termed XPCB-hHR23B) and compared it with the previously reported solution structures of the corresponding domain of hHR23A. The periodic positioning of proline residues in XPCB-hHR23B produced kinked alpha helices and assisted in the formation of a compact domain. Although the overall structure of the XPCB domain was similar in both XPCB-hHR23B and XPCB-hHR23A, the N-terminal part (residues 275-283) of XPCB-hHR23B was more flexible than the corresponding part of hHR23A. We tried to infer the characteristics of this flexibility through (15)N-relaxation studies. The hydrophobic surface of XPCB-hHR23B, which results from the diverse distribution of N-terminal region, might give rise to the functional pleiotropy observed in vivo for hHR23B, but not for hHR23A.

PubMed: 15885096
DOI: 10.1111/j.1742-4658.2005.04667.x

Experimental method

SOLUTION NMR