1hjx

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{{STRUCTURE_1hjx| PDB=1hjx | SCENE= }}
 
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===LIGAND-INDUCED SIGNALLING AND CONFORMATIONAL CHANGE OF THE 39 KD GLYCOPROTEIN FROM HUMAN ARTICULAR CHONDROCYTES===
 
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{{ABSTRACT_PUBMED_12775711}}
 
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==About this Structure==
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==Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes==
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[[1hjx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJX OCA].
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<StructureSection load='1hjx' size='340' side='right'caption='[[1hjx]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hjx]] is a 4 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=1HJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HJX FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hjx OCA], [https://pdbe.org/1hjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hjx RCSB], [https://www.ebi.ac.uk/pdbsum/1hjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hjx ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CH3L1_HUMAN CH3L1_HUMAN] A genetic variation in CHI3L1 is associated with susceptibility to asthma-related traits type 7 (ASRT7) [MIM:[https://omim.org/entry/611960 611960]. Asthma-related traits include clinical symptoms of asthma, such as coughing, wheezing and dyspnea, bronchial hyperresponsiveness (BHR) as assessed by methacholine challenge test, serum IgE levels, atopy, and atopic dermatitis.
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== Function ==
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[https://www.uniprot.org/uniprot/CH3L1_HUMAN CH3L1_HUMAN] Carbohydrate-binding lectin with a preference for chitin. May play a role in defense against pathogens, or in tissue remodeling. May play an important role in the capacity of cells to respond to and cope with changes in their environment.<ref>PMID:9492324</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/1hjx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1hjx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 39-kDa human cartilage glycoprotein (HCGP39), a member of a novel family of chitinase-like lectins (Chilectins), is overexpressed in articular chondrocytes and certain cancers. Proposed functions of this protein include a role in connective tissue remodeling and defense against pathogens. Similar to other Chi-lectins, HCGP39 promotes the growth of connective tissue cells. The ability of HCGP39 to activate cytoplasmic signaling pathways suggests the presence of a ligand for this protein at the cell surface. There is currently no information regarding the identity of any physiological or pathological ligands of the Chi-lectins or the nature of the protein-ligand interaction. Here, we show that HCGP39 is able to bind chitooligosaccharides with micromolar affinity. Crystal structures of the native protein and a complex with GlcNAc8 show that the ligand is bound in identical fashion to family 18 chitinases. However, unlike the chitinases, binding of the oligosaccharide ligand to HCGP39 induces a large conformational change. Thus, HCGP39 could be a lectin that binds chitin-like oligosaccharide ligands and possibly plays a role in innate responses to chitinous pathogens, such as fungi and nematodes.
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Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes.,Houston DR, Recklies AD, Krupa JC, van Aalten DM J Biol Chem. 2003 Aug 8;278(32):30206-12. Epub 2003 May 29. PMID:12775711<ref>PMID:12775711</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1hjx" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Chitinase-3-like protein 1|Chitinase-3-like protein 1]]
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*[[Chitinase-3-like protein 3D structures|Chitinase-3-like protein 3D structures]]
*[[Molecular Playground/YKL-40|Molecular Playground/YKL-40]]
*[[Molecular Playground/YKL-40|Molecular Playground/YKL-40]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:012775711</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Aalten, D M.F Van.]]
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[[Category: Large Structures]]
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[[Category: Houston, D R.]]
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[[Category: Houston DR]]
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[[Category: Krupa, J C.]]
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[[Category: Krupa JC]]
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[[Category: Recklies, A D.]]
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[[Category: Recklies AD]]
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[[Category: Arthristi]]
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[[Category: Van Aalten DMF]]
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[[Category: Chi-lectin]]
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[[Category: Chitinase]]
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[[Category: Chondrocyte]]
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[[Category: Lectin]]
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Current revision

Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes

PDB ID 1hjx

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