Unraveling hot spots in binding interfaces: progress and challenges.

By W. Delano. Current Opinion in Structural Biology, 2002

691 citations recorded by the source corpus.

Subfields: Computational Theory and Mathematics, Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/7381e7a2a76a4cdc5bd9fe76d898067c80029e21

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Citations in the corpus

Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. (2003, background): “Recently, it has been recognized that mutations may perturb the complex (as generally assumed), as well as the unbound states.(25) In the latter case, without additional structural information, interpreting energetic consequences of the mutations in terms of changes in binding interactions will thus”
Prediction‐based fingerprints of protein–protein interactions (2006, background): “11 In addition, amino acid biases and various physical criteria were used to identify distinct types of complexes, including transient versus obligatory and enzyme-binding versus other complexes.”
Small-molecule inhibitors of protein–protein interactions: progressing towards the dream (2004, background): “However, it might not be necessary for a small molecule to cover the entire protein-binding surface, because the subset of the interface that contributes to high-affinity binding (the 'hot spot') is often much smaller ( Box 1”
Exploiting sequence and structure homologs to identify protein–protein binding sites (2005, positive): “7,8 A small subset of residues at the interfaces form energy hot spots, enriched in tyrosine, tryptophan, and arginine.”
Protein–Protein Interaction Hotspots Carved into Sequences (2007, background): “These residues may be instrumental in understanding the interaction and could be desired drug targets [7].”
Deciphering Protein–Protein Interactions. Part I. Experimental Techniques and Databases (2007, background): “significantly to the free energy of binding [11–13].”
Protein–protein interaction and quaternary structure (2008, result): “Similar results have been obtained in other systems (Bogan & Thorn, 1998 ; DeLano, 2002).”
Fragment-based identification of druggable 'hot spots' of proteins using Fourier domain correlation techniques (2009, background): “Such regions are more likely to bind small drug-like compounds with high afﬁnity than the rest of the binding site, and hence their identiﬁcation is important for drug design (DeLano, 2002; Vajda and Guarnieri, 2006).”