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Article

Combining different design strategies for rational affinity maturation of the MICA-NKG2D interface.

Protein science : a publication of the Protein Society - 1 Sept 2012

Henager Samuel H, Hale Melissa A, Maurice Nicholas J, Dunnington Erin C, Swanson Carter J, Peterson Megan J, Ban Joseph J, Culpepper David J, Davies Luke D, Sanders Lisa K, McFarland Benjamin J

Abstract excerpt

We redesigned residues on the surface of MICA, a protein that binds the homodimeric immunoreceptor NKG2D, to increase binding affinity with a series of rational, incremental changes. A fixed-backbone RosettaDesign protocol scored a set of initial mutations, which we tested by surface plasmon resonance for thermodynamics and kinetics of NKG2D binding, both singly and in combination. We combined the best four...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 22761154
DOI: 10.1002/pro.2115
PMCID: PMC3631368

Genes

MICA

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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