1guv

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[[Category: lectin]]
[[Category: lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:15:30 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:19:56 2007''

Revision as of 13:15, 30 October 2007


1guv, resolution 2.35Å

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STRUCTURE OF HUMAN CHITOTRIOSIDASE

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, ... [(full description)]

About this Structure

1GUV is a [Single protein] structure of sequence from [Homo sapiens] with EDO as [ligand]. Structure known Active Site: EGA. 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

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