This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1lg2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lg2.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1lg2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lg2| PDB=1lg2 | SCENE= }}
{{STRUCTURE_1lg2| PDB=1lg2 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF HUMAN CHITOTRIOSIDASE IN COMPLEX WITH ETHYLENE GLYCOL'''
+
===CRYSTAL STRUCTURE OF HUMAN CHITOTRIOSIDASE IN COMPLEX WITH ETHYLENE GLYCOL===
-
==Overview==
+
<!--
-
Chitin hydrolases have been identified in a variety of organisms ranging from bacteria to eukaryotes. They have been proposed to be possible targets for the design of novel chemotherapeutics against human pathogens such as fungi and protozoan parasites as mammals were not thought to possess chitin-processing enzymes. Recently, a human chitotriosidase was described as a marker for Gaucher disease with plasma levels of the enzyme elevated up to 2 orders of magnitude. The chitotriosidase was shown to be active against colloidal chitin and is inhibited by the family 18 chitinase inhibitor allosamidin. Here, the crystal structure of the human chitotriosidase and complexes with a chitooligosaccharide and allosamidin are described. The structures reveal an elongated active site cleft, compatible with the binding of long chitin polymers, and explain the inactivation of the enzyme through an inherited genetic deficiency. Comparison with YM1 and HCgp-39 shows how the chitinase has evolved into these mammalian lectins by the mutation of key residues in the active site, tuning the substrate binding specificity. The soaking experiments with allosamidin and chitooligosaccharides give insight into ligand binding properties and allow the evaluation of differential binding and design of species-selective chitinase inhibitors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11960986}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11960986 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11960986}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Chitinase]]
[[Category: Chitinase]]
[[Category: Gaucher]]
[[Category: Gaucher]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:53:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:51:26 2008''

Revision as of 17:51, 2 July 2008

Image:1lg2.png

Template:STRUCTURE 1lg2

CRYSTAL STRUCTURE OF HUMAN CHITOTRIOSIDASE IN COMPLEX WITH ETHYLENE GLYCOL

Template:ABSTRACT PUBMED 11960986

About this Structure

1LG2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins., Fusetti F, von Moeller H, Houston D, Rozeboom HJ, Dijkstra BW, Boot RG, Aerts JM, van Aalten DM, J Biol Chem. 2002 Jul 12;277(28):25537-44. Epub 2002 Apr 17. PMID:11960986

Page seeded by OCA on Wed Jul 2 20:51:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lg2"
Personal tools