1lg2

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[[Image:1lg2.jpg|left|200px]]<br /><applet load="1lg2" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lg2, resolution 2.10&Aring;" />
 
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'''CRYSTAL STRUCTURE OF HUMAN CHITOTRIOSIDASE IN COMPLEX WITH ETHYLENE GLYCOL'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF HUMAN CHITOTRIOSIDASE IN COMPLEX WITH ETHYLENE GLYCOL==
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Chitin hydrolases have been identified in a variety of organisms ranging, from bacteria to eukaryotes. They have been proposed to be possible, targets for the design of novel chemotherapeutics against human pathogens, such as fungi and protozoan parasites as mammals were not thought to, possess chitin-processing enzymes. Recently, a human chitotriosidase was, described as a marker for Gaucher disease with plasma levels of the enzyme, elevated up to 2 orders of magnitude. The chitotriosidase was shown to be, active against colloidal chitin and is inhibited by the family 18, chitinase inhibitor allosamidin. Here, the crystal structure of the human, chitotriosidase and complexes with a chitooligosaccharide and allosamidin, are described. The structures reveal an elongated active site cleft, compatible with the binding of long chitin polymers, and explain the, inactivation of the enzyme through an inherited genetic deficiency., Comparison with YM1 and HCgp-39 shows how the chitinase has evolved into, these mammalian lectins by the mutation of key residues in the active, site, tuning the substrate binding specificity. The soaking experiments, with allosamidin and chitooligosaccharides give insight into ligand, binding properties and allow the evaluation of differential binding and, design of species-selective chitinase inhibitors.
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<StructureSection load='1lg2' size='340' side='right'caption='[[1lg2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lg2]] 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=1LG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LG2 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]] 2.1&#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=EDO:1,2-ETHANEDIOL'>EDO</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=1lg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lg2 OCA], [https://pdbe.org/1lg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lg2 RCSB], [https://www.ebi.ac.uk/pdbsum/1lg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lg2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CHIT1_HUMAN CHIT1_HUMAN] Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity.<ref>PMID:7592832</ref> <ref>PMID:7836450</ref> <ref>PMID:9748235</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/lg/1lg2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1lg2 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1LG2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LG2 OCA].
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*[[Chitinase 3D structures|Chitinase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins., Fusetti F, von Moeller H, Houston D, Rozeboom HJ, Dijkstra BW, Boot RG, Aerts JM, van Aalten DM, J Biol Chem. 2002 Jul 12;277(28):25537-44. Epub 2002 Apr 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11960986 11960986]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Dijkstra BW]]
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[[Category: Fusetti, F.]]
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[[Category: Fusetti F]]
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[[Category: Rozeboom, H.J.]]
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[[Category: Rozeboom HJ]]
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[[Category: EDO]]
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[[Category: chitin]]
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[[Category: chitinase]]
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[[Category: gaucher]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:18:02 2008''
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Current revision

CRYSTAL STRUCTURE OF HUMAN CHITOTRIOSIDASE IN COMPLEX WITH ETHYLENE GLYCOL

PDB ID 1lg2

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