A survey of the year 2006 literature on applications of isothermal titration calorimetry

Okhrimenko, Oksana; Jelesarov, Ilian

doi:10.1002/jmr.859

Cited by 29 publications

(18 citation statements)

References 418 publications

(16 reference statements)

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“…The BC-box protein had slightly lower affinity (K d = 2.2 µM), but the ΔPPL protein displayed an affinity similar to the wild type (1.25 µM). This suggests that the modest but reproducible affinity decrease measured for the BC-box protein may not be a specific effect of binding, but rather may reflect size-related properties of the truncation, possibly related to the diffusion rate in solution [29].…”

Section: Resultsmentioning

confidence: 95%

The SOCS-Box of HIV-1 Vif Interacts with ElonginBC by Induced-Folding to Recruit Its Cul5-Containing Ubiquitin Ligase Complex

et al. 2010

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The HIV-1 viral infectivity factor (Vif) protein recruits an E3 ubiquitin ligase complex, comprising the cellular proteins elongin B and C (EloBC), cullin 5 (Cul5) and RING-box 2 (Rbx2), to the anti-viral proteins APOBEC3G (A3G) and APOBEC3F (A3F) and induces their polyubiquitination and proteasomal degradation. In this study, we used purified proteins and direct in vitro binding assays, isothermal titration calorimetry and NMR spectroscopy to describe the molecular mechanism for assembly of the Vif-EloBC ternary complex. We demonstrate that Vif binds to EloBC in two locations, and that both interactions induce structural changes in the SOCS box of Vif as well as EloBC. In particular, in addition to the previously established binding of Vif's BC box to EloC, we report a novel interaction between the conserved Pro-Pro-Leu-Pro motif of Vif and the C-terminal domain of EloB. Using cell-based assays, we further show that this interaction is necessary for the formation of a functional ligase complex, thus establishing a role of this motif. We conclude that HIV-1 Vif engages EloBC via an induced-folding mechanism that does not require additional co-factors, and speculate that these features distinguish Vif from other EloBC specificity factors such as cellular SOCS proteins, and may enhance the prospects of obtaining therapeutic inhibitors of Vif function.

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Section: Resultsmentioning

confidence: 95%

The SOCS-Box of HIV-1 Vif Interacts with ElonginBC by Induced-Folding to Recruit Its Cul5-Containing Ubiquitin Ligase Complex

et al. 2010

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“…[1][2][3][4] The underlying principle is simple: the system at hand, for instance, a macromolecular solution, is titrated by small aliquots of a titrant such as a ligand solution while the temperature of the system is maintained constant. The heat supplied to or removed from the system upon each addition is recorded as being the heat effect associated with the titrant addition.…”

Section: Introductionmentioning

confidence: 99%

Quantitatively Interpreting Thermal Behavior of Self-Associating Systems

et al. 2009

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A general method is presented to extract thermodynamic as well as structural information from calorimetric data on self-associating systems using existing statistical thermodynamic models. The method is illustrated with one simple and one complex ligand binding system taken from the literature. The method is also used to extract the aggregation number using a simple mass balance model for self-assembly of surfactant molecules, and experimental evidence is provided to support this.

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“…Isothermal titration calorimetry can be used to measure the kinetics and thermodynamic constants of a binding reaction Ladbury, 2006, 2007;Okhrimenko et al, 2008). It can be seen from the kinetic results that the binding strengths of OA and LA to β-LG were similar, even though there were more binding sites for OA on β-LG than there were for LA.…”

Section: Discussionmentioning

confidence: 99%

Self-assembled β-lactoglobulin–oleic acid and β-lactoglobulin–linoleic acid complexes with antitumor activities

Fang

Zhang

Tian

et al. 2015

Journal of Dairy Science

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β-Lactoglobulin (β-LG) can bind to fatty acids such as oleic acid (OA) and linoleic acid (LA). Another whey protein, α-lactalbumin (α-LA), can also bind to OA to give the complex α-LA-OA, which has antitumor properties. Based on reports that the activity of α-LA-OA is highly dependent on OA, as well as the acquisition of similar complexes using other proteins, such as lysozyme and lactoferrin, we speculated whether β-LG could also kill tumor cells after binding to other fatty acids. Therefore, we prepared complexes of β-LG with OA (β-LG-OA) and LA (β-LG-LA) in the current study and evaluated them in terms of antitumor activity and thermostability using the methylene blue method and differential scanning calorimetry, respectively. The structural features of these complexes were also evaluated using fluorescence spectroscopy and circular dichroism. The binding dynamics of OA and LA to β-LG were studied using isothermal titration calorimetry. Cell viability results revealed that β-LG-LA and β-LG-OA exhibited similar antitumor activities. Interestingly, the binding of β-LG to LA led to an increase in its thermostability, whereas its binding to OA had very little effect. The environments of the tryptophan residues in the β-LG-OA and β-LG-LA complexes were very different, with the residues being blue- and red-shifted, respectively. Furthermore, the hydrophobic regions in β-LG were buried after binding of OA, which was slightly changed in β-LG-LA. Circular dichroism results showed that β-LG-OA enhanced the tertiary structure, which was partially lost in β-LG-LA. There were more binding sites for OA than for LA on β-LG, although the binding constants of the 2 fatty acids were similar, with both acids interacting with the protein though van der Waals and hydrogen bonding interactions. This study could help provide a deeper understanding of the structural basis for formation of antitumor protein-fatty acid complexes.

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A survey of the year 2006 literature on applications of isothermal titration calorimetry

Cited by 29 publications

References 418 publications

The SOCS-Box of HIV-1 Vif Interacts with ElonginBC by Induced-Folding to Recruit Its Cul5-Containing Ubiquitin Ligase Complex

The SOCS-Box of HIV-1 Vif Interacts with ElonginBC by Induced-Folding to Recruit Its Cul5-Containing Ubiquitin Ligase Complex

Quantitatively Interpreting Thermal Behavior of Self-Associating Systems

Self-assembled β-lactoglobulin–oleic acid and β-lactoglobulin–linoleic acid complexes with antitumor activities

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