1ghg

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{{STRUCTURE_1ghg| PDB=1ghg | SCENE= }}
{{STRUCTURE_1ghg| PDB=1ghg | SCENE= }}
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'''CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON'''
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===CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON===
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==Overview==
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The sugar residues of the glycopeptide antibiotic vancomycin contribute to the cooperativity of ligand binding, thereby increasing ligand affinity and enhancing antimicrobial activity. To assess the structural basis for these effects, we determined a 0.98 A X-ray crystal structure of the vancomycin aglycon and compared it to structures of several intact vancomycin:ligand complexes. The crystal structure reveals that the aglycon binds acetate anions and forms back-to-back dimeric complexes in a manner similar to that of intact vancomycin. However, the four independent copies of the aglycon in each asymmetric unit of the crystal exhibit a high degree of conformational heterogeneity. These results suggest that the sugar residues, in addition to enlarging and strengthening the dimer interface, provide steric constraints that limit the vancomycin molecule to a relatively small number of productive conformations.
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(as it appears on PubMed at http://www.pubmed.gov), where 11356118 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11356118}}
==About this Structure==
==About this Structure==
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[[Category: Aglycon]]
[[Category: Aglycon]]
[[Category: Glycopeptide antibiotic]]
[[Category: Glycopeptide antibiotic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:33:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:17:30 2008''

Revision as of 02:17, 1 July 2008

Template:STRUCTURE 1ghg

CRYSTAL STRUCTURE OF VANCOMYCIN AGLYCON

Template:ABSTRACT PUBMED 11356118

About this Structure

Full crystallographic information is available from OCA.

Reference

The role of sugar residues in molecular recognition by vancomycin., Kaplan J, Korty BD, Axelsen PH, Loll PJ, J Med Chem. 2001 May 24;44(11):1837-40. PMID:11356118

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