DP00573_C004: Protein VP2 [cleavage product 4]FASTA viewXML view

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
         |          |          |          |          |          |
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



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.

Region 1: 1-5 Region 2: 130-132

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.


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:
  1. X-ray crystallography

References:
  1. 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:
 



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:
  1. X-ray crystallography

References:
  1. 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.




References

  1. 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

  2. Cheung A, DeLamarter J, Weiss S, K├╝pper 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



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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