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1vf8

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{{Seed}}
 
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[[Image:1vf8.png|left|200px]]
 
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==The Crystal Structure of Ym1 at 1.31 A Resolution==
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The line below this paragraph, containing "STRUCTURE_1vf8", creates the "Structure Box" on the page.
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<StructureSection load='1vf8' size='340' side='right'caption='[[1vf8]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1vf8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VF8 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.31&#8491;</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=1vf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vf8 OCA], [https://pdbe.org/1vf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vf8 RCSB], [https://www.ebi.ac.uk/pdbsum/1vf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vf8 ProSAT]</span></td></tr>
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{{STRUCTURE_1vf8| PDB=1vf8 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CHIL3_MOUSE CHIL3_MOUSE] Lectin that binds saccharides with a free amino group, such as glucosamine or galactosamine. Binding to oligomeric saccharides is much stronger than binding to mono- or disaccharides. Also binds chitin and heparin. Has weak hexosaminidase activity but no chitinase activity. Has chemotactic activity for T-lymphocytes, bone marrow cells and eosinophils. May play a role in inflammation and allergy.<ref>PMID:10625674</ref> <ref>PMID:11297523</ref> <ref>PMID:11733538</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/vf/1vf8_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=1vf8 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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Upon nematode infection, murine peritoneal macrophages synthesize and secrete large amounts of the Ym1 protein, which is a unique functional marker for alternatively activated macrophages in T(H)2-mediated inflammatory responses. Ym1 shares significant structural similarity to the family 18 chitinases. Previously, Ym1 has been studied with respect to its carbohydrate-binding ability and glycosyl hydrolysis activity and this has led to various inconclusive interpretations. Our present co-crystallization and soaking experiments with various glucosamine or N-acetylglucosamine oligomers yield only the uncomplexed Ym1. The refined Ym1 structure at 1.31A resolution clearly displays a water cluster forming an extensive hydrogen bond network with the "active-site" residues. This water cluster contributes notable electron density to lower resolution maps and this might have misled and given rise to a previous proposal for a monoglucosamine-binding site for Ym1. A structural comparison of family 18 glycosidase (-like) proteins reveals a lack of several conserved residues in Ym1, and illustrates the versatility of the divergent active sites. Therefore, Ym1 may lack N-acetylglucosamine-binding affinity, and this suggests that a new direction should be taken to unravel the function of Ym1.
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===The Crystal Structure of Ym1 at 1.31 A Resolution===
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The crystal structure of Ym1 at 1.31 A resolution.,Tsai ML, Liaw SH, Chang NC J Struct Biol. 2004 Dec;148(3):290-6. PMID:15522777<ref>PMID:15522777</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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The line below this paragraph, {{ABSTRACT_PUBMED_15522777}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1vf8" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15522777 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15522777}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1VF8 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VF8 OCA].
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==Reference==
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<ref group="xtra">PMID:15522777</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Chang, N C.]]
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[[Category: Chang NC]]
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[[Category: Liaw, S H.]]
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[[Category: Liaw SH]]
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[[Category: Tsai, M L.]]
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[[Category: Tsai ML]]
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[[Category: Chi-lectin]]
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[[Category: Chitinase]]
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[[Category: Functional versatility]]
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[[Category: Structural plasticity]]
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[[Category: Ym1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:44:10 2009''
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Current revision

The Crystal Structure of Ym1 at 1.31 A Resolution

PDB ID 1vf8

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