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| - | [[Image:1lcl.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1lcl| PDB=1lcl | SCENE= }} | | {{STRUCTURE_1lcl| PDB=1lcl | SCENE= }} |
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| - | '''CHARCOT-LEYDEN CRYSTAL PROTEIN'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8747464}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8747464 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8747464}} |
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| | ==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]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:47:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:21:53 2008'' |
Revision as of 09:22, 2 July 2008
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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