2006
DOI: 10.1021/bi060091y
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Structural Insight into the Binding Diversity between the Human Nck2 SH3 Domains and Proline-Rich Proteins,

Abstract: Human Nck2 (hNck2) is a 380-residue adapter protein consisting of three SH3 domains and one SH2 domain. Nck2 plays a pivotal role in connecting and integrating signaling networks constituted by transmembrane receptors such as ephrinB and effectors critical for cytoskeletonal dynamics and remodeling. In this study, we aimed to determine the NMR structures and dynamic properties of the hNck2 SH3 domains and to define their ligand binding preferences with nine proline-rich peptides derived from Wire, CAP-1, CAP-2… Show more

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Cited by 37 publications
(71 citation statements)
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“…Because the E ␤-strand and the D-E and J-K loops have been previously shown to be key components of the high affinity ephrin binding channel of the Eph receptors, the NMR titration results thus suggest that the two molecules bind to the high affinity ephrin binding channel of EphA4. We also attempted to estimate the dissociation constants for the binding of the two compounds by fitting the HSQC peak tracings at different compound concentrations (44). However, accurate data fitting was impossible because at high compound concentrations the HSQC peaks for the residues with large shifts disappeared.…”
Section: Resultsmentioning
confidence: 99%
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“…Because the E ␤-strand and the D-E and J-K loops have been previously shown to be key components of the high affinity ephrin binding channel of the Eph receptors, the NMR titration results thus suggest that the two molecules bind to the high affinity ephrin binding channel of EphA4. We also attempted to estimate the dissociation constants for the binding of the two compounds by fitting the HSQC peak tracings at different compound concentrations (44). However, accurate data fitting was impossible because at high compound concentrations the HSQC peaks for the residues with large shifts disappeared.…”
Section: Resultsmentioning
confidence: 99%
“…Binding Characterization by Isothermal Titration Calorimetry and Circular Dichroism-Isothermal titration calorimetry experiments were performed using a Microcal VP isothermal titration calorimetry machine as described previously (44). Titrations were conducted in 10 mM phosphate buffer, pH 6.3, at 25°C.…”
Section: Methodsmentioning
confidence: 99%
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