1lcl
From Proteopedia
(New page: 200px<br /> <applet load="1lcl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lcl, resolution 1.8Å" /> '''CHARCOT-LEYDEN CRYST...) |
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| - | [[Image:1lcl.gif|left|200px]]<br /> | + | [[Image:1lcl.gif|left|200px]]<br /><applet load="1lcl" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1lcl" size=" | + | |
caption="1lcl, resolution 1.8Å" /> | caption="1lcl, resolution 1.8Å" /> | ||
'''CHARCOT-LEYDEN CRYSTAL PROTEIN'''<br /> | '''CHARCOT-LEYDEN CRYSTAL PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: The Charcot-Leyden crystal (CLC) protein is a major | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LCL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Lysophospholipase Lysophospholipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.5 3.1.1.5] Full crystallographic information is available from [http:// | + | 1LCL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Lysophospholipase Lysophospholipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.5 3.1.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LCL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lysophospholipase]] | [[Category: Lysophospholipase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Acharya, K | + | [[Category: Acharya, K R.]] |
| - | [[Category: Leonidas, D | + | [[Category: Leonidas, D D.]] |
[[Category: charcot-leyden crystal protein]] | [[Category: charcot-leyden crystal protein]] | ||
[[Category: serine esterase]] | [[Category: serine esterase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:42 2008'' |
Revision as of 11:43, 21 February 2008
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CHARCOT-LEYDEN CRYSTAL PROTEIN
Contents |
Overview
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.
Disease
Known disease associated with this structure: Cold-induced sweating syndrome 1 OMIM:[607672]
About 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.
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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