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1vf8

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[[Image:1vf8.gif|left|200px]]
[[Image:1vf8.gif|left|200px]]
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{{Structure
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|PDB= 1vf8 |SIZE=350|CAPTION= <scene name='initialview01'>1vf8</scene>, resolution 1.31&Aring;
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{{STRUCTURE_1vf8| PDB=1vf8 | SCENE= }}
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|RELATEDENTRY=[[1e9l|1E9L]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vf8 OCA], [http://www.ebi.ac.uk/pdbsum/1vf8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vf8 RCSB]</span>
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'''The Crystal Structure of Ym1 at 1.31 A Resolution'''
'''The Crystal Structure of Ym1 at 1.31 A Resolution'''
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[[Category: Liaw, S H.]]
[[Category: Liaw, S H.]]
[[Category: Tsai, M L.]]
[[Category: Tsai, M L.]]
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[[Category: chi-lectin]]
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[[Category: Chi-lectin]]
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[[Category: chitinase]]
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[[Category: Chitinase]]
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[[Category: functional versatility]]
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[[Category: Functional versatility]]
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[[Category: structural plasticity]]
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[[Category: Structural plasticity]]
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[[Category: ym1]]
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[[Category: Ym1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:28:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:23:33 2008''
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Revision as of 09:28, 3 May 2008

Template:STRUCTURE 1vf8

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 Page seeded by OCA on Sat May 3 12:28:18 2008

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