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Article

A proline to glycine mutation in the Lck SH3-domain affects conformational sampling and increases ligand binding affinity.

FEBS letters - 17 Apr 2007

Bauer Finn, Sticht Heinrich

Abstract excerpt

Loop flexibility is discussed as a factor that affects ligand binding affinity of SH3 domains. To test this hypothesis, we designed a mutant in which a proline in the RT-loop of the human Lck SH3-domain is replaced by glycine. The dynamics and ligand binding properties of wild-type and mutant LckSH3 were studied by fluorescence and NMR spectroscopy as well as molecular dynamics simulations. Although the mutated...

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Share to Glycine
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Share to Lymphocyte Specific Protein Tyrosine Kinase p56(lck)

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17382937
DOI: 10.1016/j.febslet.2007.03.012

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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