Crystallization of the head and galectin-like domains of porcine adenovirus isolate NADC-1 fibre

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt 11):1149-52. doi: 10.1107/S1744309109038287. Epub 2009 Oct 30.

Abstract

The porcine adenovirus NADC-1 isolate, a strain of porcine adenovirus type 4, has a fibre with an atypical architecture. In addition to a classical virus attachment region, shaft and head domains, it contains an additional galectin like domain C-terminal to the head domain and connected to the head domain by a long RGD-containing loop. The galectin-like domain contains two putative carbohydrate-recognition domains. The head and galectin-like domains have been independently crystallized. Diffraction data have been obtained to 3.2 angstrom resolution from crystals of the head domain and to 1.9 angstrom resolution from galectin-like domain crystals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Galectins / chemistry*
  • Galectins / genetics
  • Humans
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Swine
  • Viral Structural Proteins / chemistry*
  • Viral Structural Proteins / genetics
  • X-Ray Diffraction

Substances

  • Galectins
  • Viral Structural Proteins
  • fiber protein NADC-1, Porcine adenovirus