1R9W
Crystal Structure of the DNA-binding domain of the human papillomavirus type 18 (HPV-18) replication initiation protein E1
1R9W の概要
| エントリーDOI | 10.2210/pdb1r9w/pdb |
| 分子名称 | Replication protein E1 (2 entities in total) |
| 機能のキーワード | hpv-18, papillomavirus, dna-binding domain, viral replication, initiator protein, replication |
| 由来する生物種 | Human papillomavirus type 18 |
| 細胞内の位置 | Host nucleus: P06789 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 16335.23 |
| 構造登録者 | |
| 主引用文献 | Auster, A.S.,Joshua-Tor, L. The DNA-binding domain of human papillomavirus type 18 E1. Crystal structure, dimerization, and DNA binding. J.Biol.Chem., 279:3733-3742, 2004 Cited by PubMed Abstract: High risk types of human papillomavirus, such as type 18 (HPV-18), cause cervical carcinoma, one of the most frequent causes of cancer death in women worldwide. DNA replication is one of the central processes in viral maintenance, and the machinery involved is an excellent target for the design of antiviral therapy. The papillomaviral DNA replication initiation protein E1 has origin recognition and ATP-dependent DNA melting and helicase activities, and it consists of a DNA-binding domain and an ATPase/helicase domain. While monomeric in solution, E1 binds DNA as a dimer. Dimerization occurs via an interaction of hydrophobic residues on a single alpha-helix of each monomer. Here we present the crystal structure of the monomeric HPV-18 E1 DNA-binding domain refined to 1.8-A resolution. The structure reveals that the dimerization helix is significantly different from that of bovine papillomavirus type 1 (BPV-1). However, we demonstrate that the analogous residues required for E1 dimerization in BPV-1 and the low risk HPV-11 are also required for HPV-18 E1. We also present evidence that the HPV-18 E1 DNA-binding domain does not share the same nucleotide and amino acid requirements for specific DNA recognition as BPV-1 and HPV-11 E1. PubMed: 14593106DOI: 10.1074/jbc.M311681200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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