DP00573_C006: Protein VP1 [cleavage product 6]FASTA viewXML view

General information
DisProt:DP00573_C006
Name:Protein VP1 [cleavage product 6]
Synonym(s):POLG_FMDVO
P1D
Virion protein 1
cleavage product 6 of Genome polyprotein [Isoform Lab]
VP1
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:211
Percent disordered:19%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
TTSAGESADP VTTTVENYGG ETQIQRRQHT DVSFIMDRFV KVTPQNQINI LDLMQIPSHT - 60
LVGALLRAST YYFSDLEIAV KHEGDLTWVP NGAPEKALDN TTNPTAYHKA PLTRLALPYT - 120
APHRVLATVY NGECRYNRNA VPNLRGDLQV LAQKVARTLP TSFNYGAIKA TRVTELLYRM - 180
KRAETYCPRP LLAIHPTEAR HKQKIVAPVK Q



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 1 is cleavage product 6 of Genome polyprotein [Isoform Lab], comprising aa 725-935 of the polyprotein.

Region 1: 133-158 Region 2: 197-211

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:antigenic loop
Location:133 - 158
Length:26
Region sequence:

ECRYNRNAVPNLRGDLQVLAQKVART

Modification type: Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Modification site
Functional subclasses: Flexible linkers/spacers
Substrate/ligand binding
Structural mortar
Protein-protein binding
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) describe a major antigenic site called 'FMDV loop' at ~aa 140-160.


Acharya et al (1989) discuss the formation of a disulfide bridge formed between VP2 aa 130 and VP1 aa 134.




Region 2
Type:Disordered - Extended
Name:C-terminal region
Location:197 - 211
Length:15
Region sequence:

TEARHKQKIVAPVKQ

Modification type: Native
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Modification site
Functional subclasses: Flexible linkers/spacers
Protein-protein binding
Structural mortar
Substrate/ligand binding
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) characterize VP1 as 213 residues long, adding residues T212 and L213 to both protein VP1 and this Region 2. UniProt's canonical sequence stops at Q211.


According to Acharya et al (1989), a minor antigenic site exists at aa 200-213.




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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