1e9l

<StructureSection load='1e9l' size='340' side='right'caption='[[1e9l]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[1e9l]] is a 1 chain structure with 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=1E9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E9L FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GCS:D-GLUCOSAMINE'>GCS</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9l OCA], [http://pdbe.org/1e9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e9l RCSB], [http://www.ebi.ac.uk/pdbsum/1e9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e9l ProSAT]</span></td></tr>

== Function ==

[[http://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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== Publication Abstract from PubMed ==

Ym1, a secretory protein synthesized by activated murine peritoneal macrophages, is a novel mammalian lectin with a binding specificity to GlcN. Lectins are responsible for carbohydrate recognition and for mediating cell-cell and cell-extracellular matrix interactions in microbes, plants, and animals. Glycosaminoglycan heparin/heparan sulfate binding ability was also detected in Ym1. We report here the three-dimensional structure of Ym1 at 2.5-A resolution by x-ray crystallography. The crystal structure of Ym1 consists of two globular domains, a beta/alpha triose-phosphate isomerase barrel domain and a small alpha + beta folding domain. A notable electron density of sugar is detected in the Ym1 crystal structure. The saccharide is located inside the triose-phosphate isomerase domain at the COOH terminal end of the beta-strands. Both hydrophilic and hydrophobic interactions are noted in the sugar-binding site in Ym1. Despite the fact that Ym1 is not a chitinase, structurally, Ym1 shares significant homology with chitinase A of Serratia marcescens. Ym1 and chitinase A have a similar carbohydrate binding cleft. This study provides new structure information, which will lead to better understanding of the biological significance of Ym1 and its putative gene members.

The crystal structure of a novel mammalian lectin, Ym1, suggests a saccharide binding site.,Sun YJ, Chang NC, Hung SI, Chang AC, Chou CC, Hsiao CD J Biol Chem. 2001 May 18;276(20):17507-14. Epub 2001 Feb 15. PMID:11278670<ref>PMID:11278670</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1e9l" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Hsiao, C D]]

[[Category: Sun, Y J]]

[[Category: Secretory]]