We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1vf8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vf8.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1vf8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vf8| PDB=1vf8 | SCENE= }}
{{STRUCTURE_1vf8| PDB=1vf8 | SCENE= }}
-
'''The Crystal Structure of Ym1 at 1.31 A Resolution'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15522777}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15522777 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15522777}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Structural plasticity]]
[[Category: Structural plasticity]]
[[Category: Ym1]]
[[Category: Ym1]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:28:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:00:54 2008''

Revision as of 12:00, 27 July 2008

Image:1vf8.png

Template:STRUCTURE 1vf8

The Crystal Structure of Ym1 at 1.31 A Resolution

Template:ABSTRACT PUBMED 15522777

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 Sun Jul 27 15:00:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vf8"
Personal tools