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.


2a8w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2a8w.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2a8w.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2a8w| PDB=2a8w | SCENE= }}
{{STRUCTURE_2a8w| PDB=2a8w | SCENE= }}
-
'''Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA) Complexed with Beta-Methyllactoside'''
+
===Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA) Complexed with Beta-Methyllactoside===
-
==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
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16326711 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16326711}}
==Disease==
==Disease==
Line 37: Line 41:
[[Category: Gta]]
[[Category: Gta]]
[[Category: Retaining]]
[[Category: Retaining]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:45:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:56:48 2008''

Revision as of 04:56, 28 July 2008

Image:2a8w.png

Template:STRUCTURE 2a8w

Contents

Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA) Complexed with Beta-Methyllactoside

Template:ABSTRACT PUBMED 16326711

Disease

Known disease associated with this structure: Blood group, ABO system OMIM:[110300]

About this Structure

2A8W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jul 28 07:56:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a8w"
Personal tools