TY - JOUR
T1 - Characterization of intramolecular interactions of HIV-1 accessory protein Nef by differential scanning calorimetry
AU - Groesch, Teresa D.
AU - Freire, Ernesto
N1 - Funding Information:
This work was supported by grants from the National Science Foundation MCB0131241 and the National Institutes of Health GM 57144 and GM56550.
Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2007/3
Y1 - 2007/3
N2 - The interactions between the N-terminal arm and the structural core of Nef, an HIV-1 accessory protein, have been studied by high sensitivity differential scanning calorimetry. Critical interactions have been identified by measuring the structural energetics of both truncation and point mutants of the protein. These studies demonstrate that the N-terminal arm of Nef strongly interacts with the core and that it contributes close to 4.3 kcal/mol to the stability of the entire protein. The interactions are not evenly distributed through the N-terminal arm. Two strongly interacting regions have been identified: the region between residues 1 and 40 that contributes 1.6 kcal/mol to the stability of Nef; and, the region between residues 50 and 61 that contributes 2.7 kcal/mol. Other regions (e.g. residues 41 to 49) appear to contribute little to the interaction. The identification of these, until now, elusive interactions provides a physical foundation for allosteric effects between N-terminal arm and protein core elicited by different binding partners.
AB - The interactions between the N-terminal arm and the structural core of Nef, an HIV-1 accessory protein, have been studied by high sensitivity differential scanning calorimetry. Critical interactions have been identified by measuring the structural energetics of both truncation and point mutants of the protein. These studies demonstrate that the N-terminal arm of Nef strongly interacts with the core and that it contributes close to 4.3 kcal/mol to the stability of the entire protein. The interactions are not evenly distributed through the N-terminal arm. Two strongly interacting regions have been identified: the region between residues 1 and 40 that contributes 1.6 kcal/mol to the stability of Nef; and, the region between residues 50 and 61 that contributes 2.7 kcal/mol. Other regions (e.g. residues 41 to 49) appear to contribute little to the interaction. The identification of these, until now, elusive interactions provides a physical foundation for allosteric effects between N-terminal arm and protein core elicited by different binding partners.
KW - AIDS
KW - Differential scanning calorimetry
KW - HIV
KW - Intraprotein interaction
KW - Nef
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U2 - 10.1016/j.bpc.2006.05.007
DO - 10.1016/j.bpc.2006.05.007
M3 - Article
C2 - 16730880
AN - SCOPUS:33846576688
SN - 0301-4622
VL - 126
SP - 36
EP - 42
JO - Biophysical Chemistry
JF - Biophysical Chemistry
IS - 1-3
ER -