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Article

Evolved streptavidin mutants reveal key role of loop residue in high-affinity binding.

Protein science : a publication of the Protein Society - 1 Jul 2011

Magalhães Maria L B, Czekster Clarissa Melo, Guan Rong, Malashkevich Vladimir N, Almo Steven C, Levy Matthew

Abstract excerpt

We have performed a detailed analysis of streptavidin variants with altered specificity towards desthiobiotin. In addition to changes in key residues which widen the ligand binding pocket and accommodate the more structurally flexible desthiobiotin, the data revealed the role of a key, non-active site mutation at the base of the flexible loop (S52G) which slows dissociation of this ligand by approximately...

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Identifiers

PMID: 21520321
DOI: 10.1002/pro.642
PMCID: PMC3149188

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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