1a7g
From Proteopedia
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THE CRYSTAL STRUCTURE OF THE E2 DNA-BINDING DOMAIN FROM HUMAN PAPILLOMAVIRUS AT 2.4 ANGSTROMS
Overview
The papillomaviruses are a family of small double-stranded DNA viruses, which exclusively infect epithelial cells and stimulate the proliferation, of those cells. A key protein within the papillomavirus life-cycle is, known as the E2 (Early 2) protein and is responsible for regulating viral, transcription from all viral promoters as well as for replication of the, papillomavirus genome in tandem with another protein known as E1. The E2, protein itself consists of three functional domains: an N-terminal, trans-activation domain, a proline-rich linker, and a C-terminal, DNA-binding domain. The first crystal structure of the human, papillomavirus, serotype 31 (HPV-31), E2 DNA-binding domain has been, determined at 2.4 A resolution. The HPV DNA-binding domain monomer, consists of two beta-alpha-beta repeats of approximately equal length and, is arranged as to have an anti-parallel beta-sheet flanked by the two, alpha-helices. The monomers form the functional in vivo dimer by, association of the beta-sheets of each monomer so as to form an, eight-stranded anti-parallel beta-barrel at the center of the dimer, with, the alpha-helices lining the outside of the barrel. The overall structure, of HVP-31 E2 DNA-binding domain is similar to both the bovine, papillomavirus E2-binding domain and the Epstein-Barr nuclear antigen-1, DNA-binding domain.
About this Structure
1A7G is a Single protein structure of sequence from Human papillomavirus type 92 with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the E2 DNA-binding domain from human papillomavirus serotype 31 at 2.4 A., Bussiere DE, Kong X, Egan DA, Walter K, Holzman TF, Lindh F, Robins T, Giranda VL, Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1367-76. PMID:10089498
Page seeded by OCA on Tue Nov 20 10:39:53 2007
