1CN3

INTERACTION OF POLYOMAVIRUS INTERNAL PROTEIN VP2 WITH MAJOR CAPSID PROTEIN VP1 AND IMPLICATIONS FOR PARTICIPATION OF VP2 IN VIRAL ENTRY

Summary for 1CN3

• Entry DOI: 10.2210/pdb1cn3/pdb
• Descriptor: COAT PROTEIN VP1, FRAGMENT OF COAT PROTEIN VP2 (2 entities in total)
• Functional Keywords: viral coat protein vp1, viral coat protein vp2, viral entry, viral protein
• Biological source: Polyomavirus; More
• Cellular location: Virion: P49302; Isoform VP2: Virion. Isoform VP3: Virion: P12908
• Total number of polymer chains: 6
• Total formula weight: 160305.21

Authors

Chen, X.,Stehle, T.,Harrison, S.C. (deposition date: 1999-05-24, release date: 1999-06-09, Last modification date: 2023-12-27)

Primary citation

Chen, X.S.,Stehle, T.,Harrison, S.C.
Interaction of polyomavirus internal protein VP2 with the major capsid protein VP1 and implications for participation of VP2 in viral entry.
EMBO J., 17:3233-3240, 1998

PubMed Abstract: A complex of the polyomavirus internal protein VP2/VP3 with the pentameric major capsid protein VP1 has been prepared by co-expression in Escherichia coli. A C-terminal segment of VP2/VP3 is required for tight association, and a crystal structure of this segment, complexed with a VP1 pentamer, has been determined at 2.2 A resolution. The structure shows specific contacts between a single copy of the internal protein and a pentamer of VP1. These interactions were not detected in the previously described structure of the virion, but the location of VP2 in the recombinant complex is consistent with features in the virion electron-density map. The C-terminus of VP2/VP3 inserts in an unusual, hairpin-like manner into the axial cavity of the VP1 pentamer, where it is anchored strongly by hydrophobic interactions. The remainder of the internal protein appears to have significant flexibility. This structure restricts possible models for exposure of the internal proteins during viral entry.

PubMed: 9628860
DOI: 10.1093/emboj/17.12.3233

Experimental method

X-RAY DIFFRACTION (2.2 Å)