PDBsum entry 2f8b

Oncoprotein, virus/viral protein

PDB id: 2f8b

Contents

Protein chains

56 a.a. *

Metals

_ZN ×2

* Residue conservation analysis

PDB id:

2f8b

Name:

Oncoprotein, virus/viral protein

Title:

Nmr structure of thE C-terminal domain (dimer) of hpv45 oncoprotein e7

Structure:

Protein e7. Chain: a, b. Fragment: c-terminal domain, residues 55-106. Engineered: yes

Source:

Human papillomavirus type 45. Organism_taxid: 10593. Strain: hpv type 45. Gene: e7. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

15 models

Authors:

O.Ohlenschlager,M.Gorlach

Key ref:

O.Ohlenschläger et al. (2006). Solution structure of the partially folded high-risk human papilloma virus 45 oncoprotein E7. Oncogene, 25, 5953-5959. PubMed id: 16636661

Date:

02-Dec-05 Release date: 08-Aug-06

Protein chains

P21736  (VE7_HPV45) -  Protein E7 from Human papillomavirus 45

Seq: 106 a.a.

Struc: 56 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

Oncogene 25:5953-5959 (2006)

PubMed id: 16636661

Solution structure of the partially folded high-risk human papilloma virus 45 oncoprotein E7.

O.Ohlenschläger, T.Seiboth, H.Zengerling, L.Briese, A.Marchanka, R.Ramachandran, M.Baum, M.Korbas, W.Meyer-Klaucke, M.Dürst, M.Görlach.

ABSTRACT

The oncoprotein E7 of human papilloma viruses (HPV) is involved in the pathogenesis and maintenance of human cervical cancers. The most prevalent HPV types found in cervix carcinomas are HPV16, 18 and 45. The structure of the E7 dimer from HPV45 (PDB 2F8B) was determined by nuclear magnetic resonance spectroscopy. Each monomer comprises an unfolded N-terminus and a well-structured C-terminal domain with a beta1beta2alpha1beta3alpha2 topology representing a unique zinc-binding fold found only for E7. Dimerization occurs through the alpha1/alpha1' helices and intermolecular beta-sheet formation but excludes the zinc-binding sites. E7 is reported to interact with a number of cellular proteins (e.g. pRb, p21(CIP1)). Binding of a peptide derived from the C-terminus of p21(CIP1) to the C-terminal domain of E7 was characterized by monitoring chemical shift perturbations of the amide groups of E7. This provides direct evidence that a shallow groove situated between alpha1 and beta1 of the E7 C-terminal domain is interacting with the C-terminus of p21(CIP1). Intriguingly, this binding site overlaps with the low-affinity binding site on E7 for the C-domain of pRb.