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| [[Image:1lcl.gif|left|200px]]<br />
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| <applet load="1lcl" size="450" color="white" frame="true" align="right" spinBox="true"
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| caption="1lcl, resolution 1.8Å" />
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| '''CHARCOT-LEYDEN CRYSTAL PROTEIN'''<br />
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| ==Overview== | | ==CHARCOT-LEYDEN CRYSTAL PROTEIN== |
| 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.
| | <StructureSection load='1lcl' size='340' side='right'caption='[[1lcl]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | | == Structural highlights == |
| ==Disease==
| | <table><tr><td colspan='2'>[[1lcl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LCL FirstGlance]. <br> |
| Known disease associated with this structure: Cold-induced sweating syndrome 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607672 607672]]
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lcl OCA], [https://pdbe.org/1lcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lcl RCSB], [https://www.ebi.ac.uk/pdbsum/1lcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lcl ProSAT]</span></td></tr> |
| ==About this Structure== | | </table> |
| 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LCL OCA].
| | == Function == |
| | | [https://www.uniprot.org/uniprot/LEG10_HUMAN LEG10_HUMAN] Regulates immune responses through the recognition of cell-surface glycans. Essential for the anergy and suppressive function of CD25-positive regulatory T-cells (Treg).<ref>PMID:17502455</ref> |
| ==Reference== | | == Evolutionary Conservation == |
| 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8747464 8747464]
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lc/1lcl_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lcl ConSurf]. |
| | <div style="clear:both"></div> |
| | == References == |
| | <references/> |
| | __TOC__ |
| | </StructureSection> |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| [[Category: Lysophospholipase]] | | [[Category: Large Structures]] |
| [[Category: Single protein]]
| | [[Category: Acharya KR]] |
| [[Category: Acharya, K.R.]] | | [[Category: Leonidas DD]] |
| [[Category: Leonidas, D.D.]] | |
| [[Category: charcot-leyden crystal protein]]
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| [[Category: serine esterase]]
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| ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:58:46 2007''
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