2a8u: Difference between revisions

Revision as of 09:23, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2a8u.png

Template:STRUCTURE 2a8u

Crystal Structure of Human Galactosyltransferase (GTB) Complexed with Beta-Methyl LactosideCrystal Structure of Human Galactosyltransferase (GTB) Complexed with Beta-Methyl Lactoside

Template:ABSTRACT PUBMED 16326711

About this StructureAbout this Structure

2A8U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases., Letts JA, Rose NL, Fang YR, Barry CH, Borisova SN, Seto NO, Palcic MM, Evans SV, J Biol Chem. 2006 Feb 10;281(6):3625-32. Epub 2005 Dec 2. PMID:16326711

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of Human Galactosyltransferase (GTB) Complexed with Beta-Methyl Lactoside'''
+===Crystal Structure of Human Galactosyltransferase (GTB) Complexed with Beta-Methyl Lactoside===
-==Overview==
+<!--
-The human ABO(H) blood group A and B antigens are generated by the homologous glycosyltransferases A (GTA) and B (GTB), which add the monosaccharides GalNAc and Gal, respectively, to the cell-surface H antigens. In the first comprehensive structural study of the recognition by a glycosyltransferase of a panel of substrates corresponding to acceptor fragments, 14 high resolution crystal structures of GTA and GTB have been determined in the presence of oligosaccharides corresponding to different segments of the type I (alpha-l-Fucp-(1--&gt;2)-beta-D-Galp-(1--&gt;3)-beta-D-GlcNAcp-OR, where R is a glycoprotein or glycolipid in natural acceptors) and type II (alpha-l-Fucp-(1--&gt;2)-beta-D-Galp-(1--&gt;4)-beta-d-GlcNAcp-OR) H antigen trisaccharides. GTA and GTB differ in only four "critical" amino acid residues (Arg/Gly-176, Gly/Ser-235, Leu/Met-266, and Gly/Ala-268). As these enzymes both utilize the H antigen acceptors, the four critical residues had been thought to be involved strictly in donor recognition; however, we now report that acceptor binding and subsequent transfer are significantly influenced by two of these residues: Gly/Ser-235 and Leu/Met-266. Furthermore, these structures show that acceptor recognition is dominated by the central Gal residue despite the fact that the L-Fuc residue is required for efficient catalysis and give direct insight into the design of model inhibitors for GTA and GTB.
+The line below this paragraph, {{ABSTRACT_PUBMED_16326711}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16326711}}
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