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| - | [[Image:1rex.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1rex| PDB=1rex | SCENE= }} | | {{STRUCTURE_1rex| PDB=1rex | SCENE= }} |
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| - | '''NATIVE HUMAN LYSOZYME'''
| + | ===NATIVE HUMAN LYSOZYME=== |
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| - | ==Overview==
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| - | In order to reveal the origin of carbohydrate recognition specificity of human lysozyme by clarifying the difference in the binding mode of ligands in the active site, the inactivation of human lysozyme by 2',3'-epoxypropyl beta-glycoside derivatives of the disaccharides, N,N'-diacetylchitobiose [GlcNAc-beta-(1-->4)-GlcNAc] and N-acetyllactosamine [Gal-beta-(1-->4)-GlcNAc], was investigated and the three-dimensional structures of the affinity-labeled enzymes were determined by X-ray crystallography at 1.7 A resolution. Under the conditions comprising 2.0 x 10(-3) M labeling reagent and 1.0 x 10(-5) M human lysozyme at pH 5.4, 37 degrees C, the reaction time required to reduce the lytic activity against Micrococcus luteus cells to 50% of its initial activity was lengthened by 3.7 times through the substitution of the nonreducing end sugar residue, GlcNAc to Gal. The refined structure of human lysozyme labeled by 2',3'-epoxypropyl beta-glycoside derivatives of N,N'-diacetylchitobiose (HL/NAG-NAG-EPO complex) indicated that the interaction mode of the N,N'-diacetylchitobiose moiety in substites B and C in this study was essentially the same as in the case of the complex of human lysozyme with the free ligand. On the other hand, the hydrogen-bonding pattern and the stacking interaction at subsite B were remarkably different between the HL/NAG-NAG-EPO complex and human lysozyme labeled by the 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine (HL/GAL-NAG-EPO complex). The reduced number of possible hydrogen bonds as well as the less favorable stacking between the side chain of Tyr63 in human lysozyme and the galactose residue in the HL/GAL-NAG-EPO complex reasonably explained the less efficient ability of the 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine as compared to that of N,N'-diacetylchitobiose as an affinity labeling reagent toward human lysozyme.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8885835}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8885835 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8885835}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Glycosydase]] | | [[Category: Glycosydase]] |
| | [[Category: Vertebrate c-type]] | | [[Category: Vertebrate c-type]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:24:40 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:21:51 2008'' |
Revision as of 21:21, 28 July 2008
Template:STRUCTURE 1rex
NATIVE HUMAN LYSOZYME
Template:ABSTRACT PUBMED 8885835
About this Structure
1REX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Origin of carbohydrate recognition specificity of human lysozyme revealed by affinity labeling., Muraki M, Harata K, Sugita N, Sato K, Biochemistry. 1996 Oct 22;35(42):13562-7. PMID:8885835
Page seeded by OCA on Tue Jul 29 00:21:51 2008
