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1lcl

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[[Image:1lcl.gif|left|200px]]
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{{STRUCTURE_1lcl| PDB=1lcl | SCENE= }}
{{STRUCTURE_1lcl| PDB=1lcl | SCENE= }}
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'''CHARCOT-LEYDEN CRYSTAL PROTEIN'''
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===CHARCOT-LEYDEN CRYSTAL PROTEIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8747464 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8747464}}
==About this Structure==
==About this Structure==
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[[Category: Charcot-leyden crystal protein]]
[[Category: Charcot-leyden crystal protein]]
[[Category: Serine esterase]]
[[Category: Serine esterase]]
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Revision as of 09:22, 2 July 2008

Image:1lcl.png

Template:STRUCTURE 1lcl

CHARCOT-LEYDEN CRYSTAL PROTEIN

Template:ABSTRACT PUBMED 8747464

About this Structure

1LCL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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