tailieunhanh - Báo cáo khoa học: Solution structure and backbone dynamics of the XPC-binding domain of the human DNA repair protein hHR23B

Human cells contain two homologs of the yeast RAD23 protein, hHR23A and hHR23B, which participate in the DNA repair process. hHR23B hou-ses 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. | ềFEBS Journal Solution structure and backbone dynamics of the XPC-binding domain of the human DNA repair protein hHR23B Byoungkook Kim1 z Kyoung-Seok Ryu2 z Hyun-Jin Kim1 Sung-Jae Cho1 and Byong-Seok Choi1 1 Department of Chemistry and NationalCreative Research Initiative Center for the Repair System of Damaged DNA Korea Advanced Institute of Science and Technology South Korea 2 Korea Basic Science Institute Daejon South Korea Keywords hHR23B nucleotide excision repair stressinducible structure xeroderma pigmentosum group C protein Correspondence . Choi Department of Chemistry and NationalCreative Research Initiative Center for Repair System of Damaged DNA Korea Advanced Institute of Science and Technology Yusong-Gu Gusong-Dong 373-1 Daejon 305-701 South Korea Fax 82 42 869 2810 Tel 82 42 869 2868 E-mail Byoungkook Kim and Kyoung-Seok Ryu contributed equally to this work Note The atomic coordinates of the bundle of 20 conformers have been deposited in the RCSB Protein Data Bank with entry code 1PVE 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 stressinducible 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 a 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 .