| General information | | DisProt: | DP00650 | | Name: | Protein Tat | | Synonym(s): | Q1PAB4_9HIV1
Protein Tat from primary isolate 133
Tat(133)
Transactivating regulatory protein
| | First appeared in release: | Release 5.2 (08/07/2010) | | UniProt: | Q1PAB4 | | UniGene: | | | SwissProt: | Q1PAB4_9HIV1 | | TrEMBL: | | | NCBI (GI): | 123954013 | | Source organism: | Human immunodeficiency virus 1 | | Sequence length: | 101 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MEPVDPRLEP WKHPGSQPRT ACTNCYCKKC CFHCQVCFIR KALGISYGRK KRRQRRRAPQ - 60
DSETHQVSPP KQPASQPRGD PTGPKESKKK VERETETHPV N
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| Functional narrative |
Among its varied functions, Tat is a transactivator of transcription of viral genes. The 101 amino acid residue protein described here is the common form of circulating Tat in infected individuals (Foucault et al. 2009)
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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 - 101 | | Length: | 101 | | Region sequence: |
MEPVDPRLEPWKHPGSQPRTACTNCYCKKCCFHCQVCFIRKALGISYGRKKRRQRRRAPQ
DSETHQVSPPKQPASQPRGDPTGPKESKKKVERETETHPVN | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Intraprotein interaction
Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (310 K; pH: 7; H20; When used, TFE or TMAO (response at 20% TFE or 2M TMAO); wt-Tat133 (alone or in presence of TFE, TMAO or urea) 0.1 mg/mL)
- Dynamic light scattering (298 K; pH: 7.5; NaCl 100 mM; wt-Tat133 1 mg/mL)
- Small-angle X-ray scattering (SAXS) (pH: 7.5; NaCl 100 mM; wt-Tat133 1 mg/mL)
- Fluorescence, intrinsic (wt-Tat133 50 ug/mL)
- Circular dichroism (CD) spectroscopy, far-UV (310 K; pH: 7; sodium phosphate 10 mM; wt-Tat133/Fab' complex 0.6 mg/mL)
- Size exclusion/gel filtration chromatography (310 K; pH: 7; NaCl 0.15 M; phosphate (buffer) 0.05 M; wt-Tat133 (Elution volume:) 11.31 mL)
| References:
- Foucault M, Mayol K, Receveur-Brechot V, Bussat MC, Klinguer-Hamour C, Verrier B, Beck A, Haser R, Gouet P, Guillon C. "UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate." Proteins. 2009. PubMed: 20034112
| Comments:In addition to wild-type Tat133, structural analysis was also performed on STLA-Tat133, an inactive mutant form proposed to be a potential vaccine candidate (Foucalt et al. 2009).
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| References |
- Foucault M, Mayol K, Receveur-Brechot V, Bussat MC, Klinguer-Hamour C, Verrier B, Beck A, Haser R, Gouet P, Guillon C. "UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate." Proteins. 2009. PubMed: 20034112
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| Comments |
AV (8-2-2010) PubMed: 20034112
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