1vf8
From Proteopedia
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| - | [[Image:1vf8.gif|left|200px]] | + | [[Image:1vf8.gif|left|200px]] |
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| - | '''The Crystal Structure of Ym1 at 1.31 A Resolution''' | + | {{Structure |
| + | |PDB= 1vf8 |SIZE=350|CAPTION= <scene name='initialview01'>1vf8</scene>, resolution 1.31Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''The Crystal Structure of Ym1 at 1.31 A Resolution''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VF8 is a [ | + | 1VF8 is a [[Single protein]] 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]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15522777 15522777] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ym1]] | [[Category: ym1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:44:44 2008'' |
Revision as of 12:44, 20 March 2008
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| , resolution 1.31Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Crystal Structure of Ym1 at 1.31 A Resolution
Overview
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.
About this Structure
1VF8 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
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