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.
1uc0
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1uc0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uc0, resolution 1.85Å" /> '''Crystal structure of...)
Next diff →
Revision as of 01:53, 21 November 2007
|
Crystal structure of wild-type hen-egg white lysozyme singly labeled with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine
Overview
In spite of the belonging to the same c-type lysozyme family, hen, egg-white lysozyme (HEWL) was much less susceptible to the dual-affinity, labeling with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine, (Galbeta1,4GlcNAc-Epo) than human lysozyme (HL). The three-dimensional, structures of the HEWL labeled with single Galbeta1,4GlcNAc-Epo and the, Glu102-mutant HL labeled with double Galbeta1,4GlcNAc-Epo were determined, by X-ray crystallography at resolutions of 1.85 and 2.0 A, respectively., The overall conformation and the interaction mode of the carbohydrate, ligand part in the singly labeled HEWL and the doubly labeled, Glu102-mutant HL were basically identical to those of the correspondingly, labeled wild-type HL with minor alterations in some stereochemical, parameters. A detailed comparison of the structures revealed the key, protein-carbohydrate and carbohydrate-carbohydrate interactions essential, for the dual labeling. It was suggested that the difference in the, efficiency of the dual labeling was caused by the structural difference, between Gln104 in HL and Asn103 in HEWL. The relevance to our previous, study and the carbohydrate-carbohydrate interaction on cell-surface, membranes were discussed.
About this Structure
1UC0 is a Single protein structure of sequence from Gallus gallus with GOL as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
X-ray structural analysis of the ligand-recognition mechanism in the dual-affinity labeling of c-type lysozyme with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine., Muraki M, Harata K, J Mol Recognit. 2003 Mar-Apr;16(2):72-82. PMID:12720276
Page seeded by OCA on Wed Nov 21 04:00:26 2007
