1zj2: Difference between revisions

New page: left|200px<br /> <applet load="1zj2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zj2, resolution 1.69Å" /> '''Crystal Structure o...
 
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[[Image:1zj2.gif|left|200px]]<br />
[[Image:1zj2.gif|left|200px]]<br /><applet load="1zj2" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1zj2" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1zj2, resolution 1.69&Aring;" />
caption="1zj2, resolution 1.69&Aring;" />
'''Crystal Structure of Human Galactosyltransferase (GTB) Complexed with H type I Trisaccharide'''<br />
'''Crystal Structure of Human Galactosyltransferase (GTB) Complexed with H type I Trisaccharide'''<br />


==Overview==
==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 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.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1ZJ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HG, CL, MN, UDP and DR3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZJ2 OCA].  
1ZJ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HG:'>HG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=UDP:'>UDP</scene> and <scene name='pdbligand=DR3:'>DR3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZJ2 OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Barry, C.H.]]
[[Category: Barry, C H.]]
[[Category: Borisova, S.N.]]
[[Category: Borisova, S N.]]
[[Category: Evans, S.V.]]
[[Category: Evans, S V.]]
[[Category: Fang, Y.R.]]
[[Category: Fang, Y R.]]
[[Category: Letts, J.A.]]
[[Category: Letts, J A.]]
[[Category: Palcic, M.M.]]
[[Category: Palcic, M M.]]
[[Category: Rose, N.L.]]
[[Category: Rose, N L.]]
[[Category: Seto, N.O.]]
[[Category: Seto, N O.]]
[[Category: CL]]
[[Category: CL]]
[[Category: DR3]]
[[Category: DR3]]
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[[Category: transferase]]
[[Category: transferase]]


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