2de0

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(New page: 200px<br /> <applet load="2de0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2de0, resolution 2.61&Aring;" /> '''Crystal structure o...)
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'''Crystal structure of human alpha 1,6-fucosyltransferase, FUT8'''<br />
'''Crystal structure of human alpha 1,6-fucosyltransferase, FUT8'''<br />
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==About this Structure==
==About this Structure==
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2DE0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Glycoprotein_6-alpha-L-fucosyltransferase Glycoprotein 6-alpha-L-fucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.68 2.4.1.68] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DE0 OCA].
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2DE0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Glycoprotein_6-alpha-L-fucosyltransferase Glycoprotein 6-alpha-L-fucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.68 2.4.1.68] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DE0 OCA].
==Reference==
==Reference==
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[[Category: sh3 domain]]
[[Category: sh3 domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:31:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:09:03 2008''

Revision as of 13:09, 23 January 2008


2de0, resolution 2.61Å

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Crystal structure of human alpha 1,6-fucosyltransferase, FUT8

Overview

FUT8, mammalian alpha1,6-fucosyltransferase, catalyses the transfer of a, fucose residue from a donor substrate, GDP-beta-L-fucose, to the reducing, terminal GlcNAc of the core structure of an asparagine-linked, oligosaccharide. alpha1,6-Fucosylation, also referred to as a core, fucosylation, plays an essential role in various pathophysiological, events. Our group reported that FUT8 null mice show severe growth, retardation and emphysema-like lung-destruction as a result of the, dysfunction of EGF and TGF-beta receptors. To elucidate the molecular, basis of FUT8 with respect to pathophysiology, the crystal structure of, human FUT8 was determined at 2.6 A resolution. The overall structure of, FUT8 was found to consist of three domains, an N-terminal coiled-coil, domain, a catalytic domain and a C-terminal SH3 domain. The catalytic, region appears to be similar to GT-B glycosyltransferases rather than, GT-A. The C-terminal part of the catalytic domain of FUT8 includes a, Rossmann fold with three regions that are conserved in alpha1,6-, alpha1,2-, and protein O-fucosyltransferases. The SH3 domain of FUT8 is, similar to other SH3 domain-containing proteins, although the significance, of this domain remains to be elucidated. The present findings of FUT8, suggest that the conserved residues in the three conserved regions, participate in the Rossmann fold and act as the donor binding site, or, catalysis, thus playing a key role in the fucose-transferring reaction.

About this Structure

2DE0 is a Single protein structure of sequence from Homo sapiens. Active as Glycoprotein 6-alpha-L-fucosyltransferase, with EC number 2.4.1.68 Full crystallographic information is available from OCA.

Reference

Crystal Structure of Mammalian {alpha}1,6-Fucosyltransferase, FUT8., Ihara H, Ikeda Y, Toma S, Wang X, Suzuki T, Gu J, Miyoshi E, Tsukihara T, Honke K, Matsumoto A, Nakagawa A, Taniguchi N, Glycobiology. 2006 Dec 15;. PMID:17172260

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