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.
|
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:
- 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) 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:
- 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) 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 |
- 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
|
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.
|
If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|