1e9l
From Proteopedia
(New page: 200px<br /><applet load="1e9l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e9l, resolution 2.5Å" /> '''THE CRYSTAL STRUCTURE...) |
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| - | [[Image:1e9l.jpg|left|200px]]<br /><applet load="1e9l" size=" | + | [[Image:1e9l.jpg|left|200px]]<br /><applet load="1e9l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e9l, resolution 2.5Å" /> | caption="1e9l, resolution 2.5Å" /> | ||
'''THE CRYSTAL STRUCTURE OF NOVEL MAMMALIAN LECTIN YM1 SUGGESTS A SACCHARIDE BINDING SITE'''<br /> | '''THE CRYSTAL STRUCTURE OF NOVEL MAMMALIAN LECTIN YM1 SUGGESTS A SACCHARIDE BINDING SITE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ym1, a secretory protein synthesized by activated murine peritoneal | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1E9L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with GCS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1E9L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=GCS:'>GCS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hsiao, C | + | [[Category: Hsiao, C D.]] |
| - | [[Category: Sun, Y | + | [[Category: Sun, Y J.]] |
[[Category: GCS]] | [[Category: GCS]] | ||
[[Category: inducible]] | [[Category: inducible]] | ||
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[[Category: secretory]] | [[Category: secretory]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:25:26 2008'' |
Revision as of 10:25, 21 February 2008
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THE CRYSTAL STRUCTURE OF NOVEL MAMMALIAN LECTIN YM1 SUGGESTS A SACCHARIDE BINDING SITE
Overview
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.
About this Structure
1E9L is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:25:26 2008
Categories: Mus musculus | Single protein | Hsiao, C D. | Sun, Y J. | GCS | Inducible | Inflammation | Lectin | Secretory
