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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, structure, function, and bioinformatics, 2010-05, Vol.78 (6), p.1441-1456
Foucault, Marine
Mayol, Katia
Receveur-Bréchot, Véronique
Bussat, Marie-Claire
Klinguer-Hamour, Christine
Verrier, Bernard
Beck, Alain
Haser, Richard
Gouet, Patrice
Guillon, Christophe
2010
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Foucault, Marine
Mayol, Katia
Receveur-Bréchot, Véronique
Bussat, Marie-Claire
Klinguer-Hamour, Christine
Verrier, Bernard
Beck, Alain
Haser, Richard
Gouet, Patrice
Guillon, Christophe
Titel
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
Ist Teil von
Proteins, structure, function, and bioinformatics, 2010-05, Vol.78 (6), p.1441-1456
Ort / Verlag
Hoboken: Wiley Subscription Services, Inc., A Wiley Company
Erscheinungsjahr
2010
Quelle
MEDLINE
Beschreibungen/Notizen
The 101‐residue long Tat protein of primary isolate 133 of the human immunodeficiency virus type 1 (HIV‐1), wt‐Tat133 displays a high transactivation activity in vitro, whereas the mutant thereof, STLA‐Tat133, a vaccine candidate for HIV‐1, has none. These two proteins were chemically synthesized and their biological activity was validated. Their structural properties were characterized using circular dichroism (CD), fluorescence emission, gel filtration, dynamic light scattering, and small angle X‐ray scattering (SAXS) techniques. SAXS studies revealed that both proteins were extended and belong to the family of intrinsically unstructured proteins. CD measurements showed that wt‐Tat133 or STLA‐Tat133 underwent limited structural rearrangements when complexed with specific fragments of antibodies. Crystallization trials have been performed on the two forms, assuming that the Tat133 proteins might have a better propensity to fold in supersaturated conditions, and small crystals have been obtained. These results suggest that biologically active Tat protein is natively unfolded and requires only a limited gain of structure for its function. Proteins 2010. © 2009 Wiley‐Liss, Inc
Sprache
Englisch
Identifikatoren
ISSN: 0887-3585
eISSN: 1097-0134
DOI: 10.1002/prot.22661
Titel-ID: cdi_hal_primary_oai_HAL_hal_00473775v1
Format
–
Schlagworte
AIDS Vaccines - chemistry
,
AIDS Vaccines - genetics
,
AIDS Vaccines - immunology
,
Amino Acid Sequence
,
Biochemistry, Molecular Biology
,
Chromatography, Gel
,
Circular Dichroism
,
Crystallography, X-Ray
,
HIV-1
,
HIV-1 - chemistry
,
HIV-1 - genetics
,
HIV-1 - isolation & purification
,
Hydrophobic and Hydrophilic Interactions
,
Immunoglobulin Fragments
,
induced folding
,
Life Sciences
,
Light
,
Methylamines
,
Molecular Sequence Data
,
Mutant Proteins - chemistry
,
natively unfolded protein
,
protein chemical synthesis
,
Protein Folding
,
SAXS
,
Scattering, Radiation
,
Scattering, Small Angle
,
Spectrophotometry, Ultraviolet
,
Tat
,
tat Gene Products, Human Immunodeficiency Virus - chemistry
,
tat Gene Products, Human Immunodeficiency Virus - genetics
,
tat Gene Products, Human Immunodeficiency Virus - immunology
,
tat Gene Products, Human Immunodeficiency Virus - metabolism
,
Trifluoroethanol
,
vaccine candidate
,
Water
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