In:
Proteins: Structure, Function, and Bioinformatics, Wiley, Vol. 78, No. 6 ( 2010-05), p. 1441-1456
Abstract:
The 101‐residue long Tat protein of primary isolate 133 of the human immunodeficiency virus type 1 (HIV‐1), wt‐Tat 133 displays a high transactivation activity in vitro , whereas the mutant thereof, STLA‐Tat 133 , 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‐Tat 133 or STLA‐Tat 133 underwent limited structural rearrangements when complexed with specific fragments of antibodies. Crystallization trials have been performed on the two forms, assuming that the Tat 133 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
Type of Medium:
Online Resource
ISSN:
0887-3585
,
1097-0134
Language:
English
Publisher:
Wiley
Publication Date:
2010
detail.hit.zdb_id:
1475032-6
SSG:
12
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