ArticleJournal of molecular biology2011
Molecular basis of a million-fold affinity maturation process in a protein-protein interaction.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Review
- Characterization of the Staphylococcal enterotoxin A: Vβ receptor interaction using human receptor fragments engineered for high affinity.Protein engineering, design & selection : PEDS · 2013Article
- Engineering a soluble high-affinity receptor domain that neutralizes staphylococcal enterotoxin C in rabbit models of disease.Protein engineering, design & selection : PEDS · 2013Article
- Combining different design strategies for rational affinity maturation of the MICA-NKG2D interface.Protein science : a publication of the Protein Society · 2012Article
- Partner-aware prediction of interacting residues in protein-protein complexes from sequence data.PloS one · 2011Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Protein engineering is becoming increasingly important for pharmaceutical applications where controlling the specificity and affinity of engineered proteins is required to create targeted protein therapeutics. Affinity increases of several thousand-fold are now routine for a variety of protein engineering approaches, and the structural and energetic bases of affinity maturation have been investigated in a number of such cases. Previously, a 3-million-fold affinity maturation process was achieved in a protein-protein interaction composed of a variant T-cell receptor fragment and a bacterial superantigen. Here, we present the molecular basis of this affinity increase. Using X-ray crystallography, shotgun reversion/replacement scanning mutagenesis, and computational analysis, we describe, in molecular detail, a process by which extrainterfacial regions of a protein complex can be rationally manipulated to significantly improve protein engineering outcomes.
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Registered trials
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