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McKenna, R, Olson, NH, Chipman, PR, Baker, TS, Booth, TF, Christensen, J, Aasted, B, Fox, JM, Bloom, ME, Wolfinbarger, JB and Agbandje-McKenna, M (1999) Three-dimensional structure of Aleutian mink disease parvovirus: implications for disease pathogenicity. J. Virol. 73:6882-91
The three-dimensional structure of expressed VP2 capsids of Aleutian mink disease parvovirus strain G (ADVG-VP2) has been determined to 22 A resolution by cryo-electron microscopy and image reconstruction techniques. A structure-based sequence alignment of the VP2 capsid protein of canine parvovirus (CPV) provided a means to construct an atomic model of the ADVG-VP2 capsid. The ADVG-VP2 reconstruction reveals a capsid structure with a mean external radius of 128 A and several surface features similar to those found in human parvovirus B19 (B19), CPV, feline panleukopenia virus (FPV), and minute virus of mice (MVM). Dimple-like depressions occur at the icosahedral twofold axes, canyon-like regions encircle the fivefold axes, and spike-like protrusions decorate the threefold axes. These spikes are not present in B19, and they are more prominent in ADV compared to the other parvoviruses owing to the presence of loop insertions which create mounds near the threefold axes. Cylindrical channels along the fivefold axes of CPV, FPV, and MVM, which are surrounded by five symmetry-related beta-ribbons, are closed in ADVG-VP2 and B19. Immunoreactive peptides made from segments of the ADVG-VP2 capsid protein map to residues in the mound structures. In vitro tissue tropism and in vivo pathogenic properties of ADV map to residues at the threefold axes and to the wall of the dimples.
Aleutian Mink Disease/pathology; Aleutian Mink Disease/virology; Aleutian Mink Disease Virus/chemistry; Aleutian Mink Disease Virus/pathogenicity; Aleutian Mink Disease Virus/ultrastructure; Amino Acid Sequence; Animals; Capsid/chemistry; Capsid/ultrastructure; Capsid Proteins; Cats; Cell Line; Cryoelectron Microscopy; Dogs; Humans; Mice; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/ultrastructure; Sequence Homology, Amino Acid; Spodoptera/cytology
|Gene product||Qualifier||GO Term||Evidence Code||with/from||Aspect||Extension||Notes||Status|
|GO:0039615: T=1 icosahedral viral capsid||
Figure 1 shows that there is formation of a capsid with T=1 symmetry. The aleutian mink disease parvovirus strain G (ADVG) capsid protein VP1 self-assembles to form a capsid with the T=1 icosahedral symmetry inside the host cell nucleus. The host in this case are minks. The paper refers to the protein as capsid protein VP2 (strain G), or ADVG-VP2, which is an isoform of of the capsid protein VP1 found in the ADVG.
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