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1d6q

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[[Image:1d6q.gif|left|200px]]
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{{Seed}}
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[[Image:1d6q.png|left|200px]]
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{{STRUCTURE_1d6q| PDB=1d6q | SCENE= }}
{{STRUCTURE_1d6q| PDB=1d6q | SCENE= }}
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'''HUMAN LYSOZYME E102 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL GLYCOSIDE OF N-ACETYLLACTOSAMINE'''
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===HUMAN LYSOZYME E102 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL GLYCOSIDE OF N-ACETYLLACTOSAMINE===
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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--&gt;Leu mutant HL labeled with 2',3'-epoxypropyl beta-glycoside of N,N'-diacetylchitobiose (L63-HL/NAG-NAG-EPO complex) and the Asp102--&gt;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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10630988 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10630988}}
==About this Structure==
==About this Structure==
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[[Category: Muramidase]]
[[Category: Muramidase]]
[[Category: N-acetyllactosamine]]
[[Category: N-acetyllactosamine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:30:41 2008''
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''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

Image:1d6q.png

Template:STRUCTURE 1d6q

HUMAN LYSOZYME E102 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL GLYCOSIDE OF N-ACETYLLACTOSAMINE

Template:ABSTRACT PUBMED 10630988

About this Structure

1D6Q 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

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