| General information | | DisProt: | DP00573_C004 | | Name: | Protein VP2 [cleavage product 4] | | Synonym(s): | POLG_FMDVO
Virion protein 2
P1B
cleavage product 4 of Genome polyprotein [Isoform Lab]
| | First appeared in release: | Release 5.4 (10/14/2010) | | UniProt: | P03305 | | UniGene: | | | SwissProt: | POLG_FMDVO | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Foot-and-mouth disease virus | | Sequence length: | 218 | | Percent disordered: | 4% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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DKKTEETTLL EDRILTTRNG HTTSTTQSSV GVTYGYATAE DFVSGPNTSG LETRVVQAER - 60
FFKTHLFDWV TSDSFGRCHL LELPTDHKGV YGSLTDSYAY MRNGWDVEVT AVGNQFNGGC - 120
LLVAMVPELY SIQKRELYQL TLFPHQFINP RTNMTAHITV PFVGVNRYDQ YKVHKPWTLV - 180
VMVVAPLTVN TEGAPQIKVY ANIAPTNVHV AGEFPSKE
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| Functional narrative |
Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. (UniProt) Virion protein 2 is cleavage product 4 of Genome polyprotein [Isoform Lab], comprising aa 287-504 of the polyprotein.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | N-terminal region | | Location: | 1 - 5 | | Length: | 5 | | Region sequence: |
DKKTE | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography
| References:
- Acharya R, Fry E, Stuart D, Fox G, Rowlands D, Brown F. "The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution." Nature. 1989; 337(6209): 709-16. PubMed: 2537470
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | FMDV loop | | Location: | 130 - 132 | | Length: | 3 | | Region sequence: |
YSI | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Intraprotein interaction
| Detection methods:
- X-ray crystallography
| References:
- Acharya R, Fry E, Stuart D, Fox G, Rowlands D, Brown F. "The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution." Nature. 1989; 337(6209): 709-16. PubMed: 2537470
| Comments:Acharya et al (1989) discuss the formation of a disulfide bridge formed between VP2 aa 130 and VP1 aa 134.
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| References |
- Acharya R, Fry E, Stuart D, Fox G, Rowlands D, Brown F. "The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution." Nature. 1989; 337(6209): 709-16. PubMed: 2537470
- Cheung A, DeLamarter J, Weiss S, Küpper H. "Comparison of the major antigenic determinants of different serotypes of foot-and-mouth disease virus." J Virol. 1983; 48(2): 451-9. PubMed: 6194313
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| Comments |
Previous entry DP00573 has been split into polyprotein (DP00573) and cleavage products (DP00573_C0XX).
Acharya et al (1989) discuss the formation of a disulfide bridge formed between VP2 aa 130 and VP1 aa 134.
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