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Article

CD44 receptor unfolding enhances binding by freeing basic amino acids to contact carbohydrate ligand.

Biophysical journal - 3 Sept 2013

Favreau Amanda J, Faller Christina E, Guvench Olgun

Abstract excerpt

The extracellular carbohydrate-binding domain of the Type I transmembrane receptor CD44 is known to undergo affinity switching, where change in conformation leads to enhanced binding of its carbohydrate ligand hyaluronan. Separate x-ray crystallographic and NMR experiments have led to competing explanations, with the former supporting minor conformational changes at the binding site and the latter a major...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 24010665
DOI: 10.1016/j.bpj.2013.07.041
PMCID: PMC3762344

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