1r9w
From Proteopedia
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Crystal Structure of the DNA-binding domain of the human papillomavirus type 18 (HPV-18) replication initiation protein E1
Overview
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.
About this Structure
1R9W is a Single protein structure of sequence from Human papillomavirus type 63. Full crystallographic information is available from OCA.
Reference
The DNA-binding domain of human papillomavirus type 18 E1. Crystal structure, dimerization, and DNA binding., Auster AS, Joshua-Tor L, J Biol Chem. 2004 Jan 30;279(5):3733-42. Epub 2003 Oct 30. PMID:14593106
Page seeded by OCA on Wed Nov 21 01:22:44 2007
