Crystallographic characterization of human eosinophil Charcot-Leyden crystals

Sieker, L.C.; Turley, S.; Trong, I. Le; Stenkamp, Ronald E.; Weller, Peter F.; Ackerman, Steven J.

doi:10.1016/0022-2836(88)90590-6

Cited by 5 publications

(1 citation statement)

References 14 publications

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“…Details of the crystallization of CLC protein during preliminary X-ray diffraction analysis have been described elsewhere [64]. Purified crystal-derived CLC protein was recrystallized using the hanging drop vapour diffusion method.…”

Section: Crystallizationmentioning

confidence: 99%

Crystal structure of human Charcot–Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins

et al. 1995

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The CLC protein structure possesses a carbohydrate-recognition domain comprising most, but not all, of the carbohydrate-binding residues that are conserved among the galectins. The protein exhibits specific (albeit weak) carbohydrate-binding activity for simple saccharides including N-acetyl-D-glucosamine and lactose. Despite CLC protein having no significant sequence or structural similarities to other lysophospholipase catalytic triad has also been identified within the CLC structure, making it a unique dual-function polypeptide. These structural findings suggest a potential intracellular and/or extracellular role(s) for the galectin-associated activities of CLC protein in eosinophil and basophil function in allergic diseases and inflammation.

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Section: Crystallizationmentioning

confidence: 99%