General information | DisProt: | DP00101_C006 | Name: | p6-gag | Synonym(s): | GAG_HV1N5
cleavage product 6 of Gag polyprotein
| First appeared in release: | Release 3.0 (02/17/2006) | UniProt: | P12493 | UniGene: | | SwissProt: | GAG_HV1N5 | TrEMBL: | | NCBI (GI): | 120839 | Source organism: | Human immunodeficiency virus type 1 (isolate NY5 group M subtype B)(HIV-1) | Sequence length: | 52 | Percent disordered: | 69% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | LQSRPEPTAP PEESFRFGEE TTTPSQKQEP IDKELYPLAS LRSLFGSDPS SQ
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Functional narrative |
p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. p6-gag is cleavage product 6 of Gag polyprotein, comprised of aa 449-500 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: | | Location: | 1 - 13 | Length: | 13 | Region sequence: |
LQSRPEPTAPPEE | Modification type: | Engineered
| PDB: | | Structural/functional type: | | Functional classes: | | Functional subclasses: | | Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7.2; Phosphate buffer; protein 0.2 mg/ml)
- Nuclear magnetic resonance (NMR) (308 K; pH: 3; H2O (super distilled); TFE-d2)
| References:
- Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U. "Solution structure of the human immunodeficiency virus type 1 p6 protein." J Biol Chem. 2005. PubMed: 16234236
| Comments:
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Region 2 | Type: | Disordered | Name: | flexible hinge region | Location: | 19 - 32 | Length: | 14 | Region sequence: |
EETTTPSQKQEPID | Modification type: | Engineered
| PDB: | | Structural/functional type: | | Functional classes: | | Functional subclasses: | | Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7.2; Phosphate buffer; protein 0.2 mg/ml)
- Nuclear magnetic resonance (NMR) (308 K; pH: 3; H2O (super distilled); TFE-d2)
| References:
- Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U. "Solution structure of the human immunodeficiency virus type 1 p6 protein." J Biol Chem. 2005. PubMed: 16234236
| Comments:
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Region 3 | Type: | Disordered | Name: | | Location: | 44 - 52 | Length: | 9 | Region sequence: |
LFGSDPSSQ | Modification type: | Engineered
| PDB: | | Structural/functional type: | | Functional classes: | | Functional subclasses: | | Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7.2; Phosphate buffer; protein 0.2 mg/ml)
- Nuclear magnetic resonance (NMR) (308 K; pH: 3; H2O (super distilled); TFE-d2)
| References:
- Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U. "Solution structure of the human immunodeficiency virus type 1 p6 protein." J Biol Chem. 2005. PubMed: 16234236
| Comments:
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Comments |
The sequence given is the sequence of the Pr55 Gag polyprotein from HIV Type 1. p6 protein is the C-terminal part of Pr55. In its mature state p6 protein is free from Pr55. This entry is for the mature free state of p6. Secondary structure, elucidated by CD and NMR spectroscopy, strongly depends on the structure-stabilizing effect of TFE.
Previous entry DP00101 has been split into polyprotein (DP00101) and cleavage product
DP00101_C006. Disorder is characterized on the cleavage product.
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