Anchor Residues in Protein–Protein Interactions

Notes on 2004 PNAS paper introducing the concept of anchor residues as key pre-configured side chains that drive protein–protein interactions. The study highlights a two-step binding mechanism, combining preformed ‘anchor’ interactions and induced-fit adjustments.

Anchor Residues in Protein–Protein Interactions

Notes on 2004 PNAS paper introducing the concept of anchor residues as key pre-configured side chains that drive protein–protein interactions. The study highlights a two-step binding mechanism, combining preformed ‘anchor’ interactions and induced-fit adjustments.

Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity

Notes on 2014 Cell paper that identifies the ‘DFG+1’ residue as a key determinant of Ser/Thr kinase phosphoacceptor specificity, with structural and biochemical validation.

Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity

Notes on 2014 Cell paper that identifies the ‘DFG+1’ residue as a key determinant of Ser/Thr kinase phosphoacceptor specificity, with structural and biochemical validation.

The Hallmark of AGC Kinase Functional Divergence is Its C-terminal Tail, a Cis-acting Regulatory Module

An elegant dissection of how the C-terminal tail (C-tail) in AGC kinases serves as a cis-acting regulatory module, driving functional divergence from other kinase families. Through conserved interactions and structural specialization, the C-tail orchestrates key regulatory processes, acting as a unique hallmark of AGC kinases.

The Hallmark of AGC Kinase Functional Divergence is Its C-terminal Tail, a Cis-acting Regulatory Module

An elegant dissection of how the C-terminal tail (C-tail) in AGC kinases serves as a cis-acting regulatory module, driving functional divergence from other kinase families. Through conserved interactions and structural specialization, the C-tail orchestrates key regulatory processes, acting as a unique hallmark of AGC kinases.

An Inherent Difference Between Serine and Threonine Phosphorylation: Phosphothreonine Strongly Prefers a Highly Ordered, Compact, Cyclic Conformation

Notes on 2023 ACS paper exploring structural differences between serine and threonine phosphorylation, focusing on phosphothreonine’s preference for ordered conformations.

An Inherent Difference Between Serine and Threonine Phosphorylation: Phosphothreonine Strongly Prefers a Highly Ordered, Compact, Cyclic Conformation

Notes on 2023 ACS paper exploring structural differences between serine and threonine phosphorylation, focusing on phosphothreonine’s preference for ordered conformations.

Molecular Mechanism Underlying Ca²⁺/Calmodulin Dependent Protein Kinase Kinase (CaMKK) Signal Transduction

An in-depth review of CaMKK signaling, including structural, regulatory, and functional insights into its activation, downstream effects, and implications for disease.

Molecular Mechanism Underlying Ca²⁺/Calmodulin Dependent Protein Kinase Kinase (CaMKK) Signal Transduction

An in-depth review of CaMKK signaling, including structural, regulatory, and functional insights into its activation, downstream effects, and implications for disease.

DFGmodel: Predicting Protein Kinase Structure in Inactive States for Structure-based Discovery of Type-II Inhibitors

Notes on 2014 ACS paper introducing DFGmodel, a computational approach to predict kinase inactive structures for type-II inhibitor discovery. Includes insights on DFG-flip and kinase conformational analysis.

DFGmodel: Predicting Protein Kinase Structure in Inactive States for Structure-based Discovery of Type-II Inhibitors

Notes on 2014 ACS paper introducing DFGmodel, a computational approach to predict kinase inactive structures for type-II inhibitor discovery. Includes insights on DFG-flip and kinase conformational analysis.

Regulation of Protein Kinases: Activation Segment Conformation and Functional Control

Notes on 2004 Molecular Cell review analyzing how activation segment conformation regulates protein kinase activity, including insights into RD pocket, anchor residues, and alternative activation mechanisms.

Regulation of Protein Kinases: Activation Segment Conformation and Functional Control

Notes on 2004 Molecular Cell review analyzing how activation segment conformation regulates protein kinase activity, including insights into RD pocket, anchor residues, and alternative activation mechanisms.

Surface Comparison Reveals Conserved Activation Mechanism in Protein Kinases

Notes on 2006_PNAS paper exploring conserved structural mechanisms of kinase activation via surface comparison.

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