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| - | [[Image:1d6p.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1d6p| PDB=1d6p | SCENE= }} | | {{STRUCTURE_1d6p| PDB=1d6p | SCENE= }} |
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| - | '''HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE'''
| + | ===HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE=== |
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| - | ==Overview==
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| - | The synergism between apolar and polar interactions in the carbohydrate recognition by human lysozyme (HL) was probed by site-directed mutagenesis and affinity labeling. The three-dimensional structures of the Tyr63-->Leu mutant HL labeled with 2',3'-epoxypropyl beta-glycoside of N,N'-diacetylchitobiose (L63-HL/NAG-NAG-EPO complex) and the Asp102-->Glu mutant HL labeled with the 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine were revealed by X-ray diffraction at 2.23 and 1.96 A resolution, respectively. Compared to the wild-type HL labeled with the 2', 3'-epoxypropyl beta-glycoside of N,N'-diacetylchitobiose, the N-acetylglucosamine residue at subsite B of the L63-HL/NAG-NAG-EPO complex markedly moved away from the 63rd residue, with substantial loss of hydrogen-bonding interactions. Evidently, the stacking interaction with the aromatic side chain of Tyr63 is essential in positioning the N-acetylglucosamine residue in the productive binding mode. On the other hand, the position of the galactose residue in subsite B of HL is almost unchanged by the mutation of Asp102 to Glu. Most hydrogen bonds, including the one between the carboxylate group of Glu102 and the axial 4-OH group of the galactose residue, were maintained by local movement of the backbone from residues 102-104. In both structures, the conformation of the disaccharide was conserved, reflecting an intrinsic conformational rigidity of the disaccharides. The structural analysis suggested that CH-pi interactions played an important role in the recognition of the carbohydrate residue at subsite B of HL. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10630988}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10630988 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10630988}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: N,n'-diacetylchitobiose]] | | [[Category: N,n'-diacetylchitobiose]] |
| | [[Category: Site-directed mutagenesis]] | | [[Category: Site-directed mutagenesis]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:30:42 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:32:49 2008'' |
Revision as of 19:32, 30 June 2008
Template:STRUCTURE 1d6p
HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE
Template:ABSTRACT PUBMED 10630988
About this Structure
1D6P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Protein-carbohydrate interactions in human lysozyme probed by combining site-directed mutagenesis and affinity labeling., Muraki M, Harata K, Sugita N, Sato KI, Biochemistry. 2000 Jan 18;39(2):292-9. PMID:10630988
Page seeded by OCA on Mon Jun 30 22:32:49 2008
