1lcl
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CHARCOT-LEYDEN CRYSTAL PROTEIN
OverviewOverview
BACKGROUND: The Charcot-Leyden crystal (CLC) protein is a major, autocrystallizing constituent of human eosinophils and basophils, comprising approximately 10% of the total cellular protein in these, granulocytes. Identification of the distinctive hexagonal bipyramidal, crystals of CLC protein in body fluids and secretions has long been, considered a hallmark of eosinophil-associated allergic inflammation., Although CLC protein possesses lysophospholipase activity, its role(s) in, eosinophil or basophil function or associated inflammatory responses has, remained speculative. RESULTS: The crystal structure of the CLC protein, has been determined at 1.8 A resolution using X-ray crystallography. The, overall structural fold of CLC protein is highly similar to that of, galectins -1 and -2, members of an animal lectin family formerly, classified as S-type or S-Lac (soluble lactose-binding) lectins. This is, the first structure of an eosinophil protein to be determined and the, highest resolution structure so far determined for any member of the, galectin family. CONCLUSIONS: 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.
DiseaseDisease
Known disease associated with this structure: Cold-induced sweating syndrome 1 OMIM:[607672]
About this StructureAbout this Structure
1LCL is a Single protein structure of sequence from Homo sapiens. Active as Lysophospholipase, with EC number 3.1.1.5 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins., Leonidas DD, Elbert BL, Zhou Z, Leffler H, Ackerman SJ, Acharya KR, Structure. 1995 Dec 15;3(12):1379-93. PMID:8747464
Page seeded by OCA on Mon Nov 12 17:58:46 2007