Document Detail


Novel fold and carbohydrate specificity of the potent anti-HIV cyanobacterial lectin from Oscillatoria agardhii.
MedLine Citation:
PMID:  20961847     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Oscillatoria agardhii agglutinin (OAA) is a recently discovered cyanobacterial lectin that exhibits potent anti-HIV activity. Up to now, only its primary structure and carbohydrate binding data have been available. To elucidate the structural basis for the antiviral mechanism of OAA, we determined the structure of this lectin by x-ray crystallography at 1.2 Å resolution and mapped the specific carbohydrate recognition sites of OAA by NMR spectroscopy. The overall architecture of OAA comprises 10 β-strands that fold into a single, compact, β-barrel-like domain, creating a unique topology compared with all known protein structures in the Protein Data Bank. OAA sugar binding was tested against Man-9 and various disaccharide components of Man-9. Two symmetric carbohydrate-binding sites were located on the protein, and a preference for Manα(1-6)Man-linked sugars was found. Altogether, our structural results explain the antiviral activity OAA and add to the growing body of knowledge about antiviral lectins.
Authors:
Leonardus M I Koharudin; William Furey; Angela M Gronenborn
Related Documents :
22564617 - Lipopolysaccharide increases monocyte binding to mesangial cells through fractalkine an...
21454587 - Glycine dimerization motif in the n-terminal transmembrane domain of the high density l...
10425537 - The oligosaccharidic component of the glycoconjugates in lichen planus, granuloma annul...
3345797 - Specific binding of lectins with the nucleus of the sea urchin embryo and changes in th...
7696507 - Protein surface-distribution and protein-protein interactions in the binding of periphe...
6733907 - Discordant inter-kit results in the radioimmunoassay for choriogonadotropin in serum.
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2010-10-19
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  286     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2011-01-10     Completed Date:  2011-03-02     Revised Date:  2014-09-17    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1588-97     Citation Subset:  IM    
Data Bank Information
Bank Name/Acc. No.:
PDB/3OBL
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Anti-HIV Agents / chemistry*,  metabolism
Binding Sites
Carbohydrates / chemistry*
Crystallography, X-Ray
Hydrophobic and Hydrophilic Interactions
Lectins / chemistry*,  metabolism
Mannose / chemistry,  metabolism
Nuclear Magnetic Resonance, Biomolecular
Oscillatoria / chemistry*
Protein Binding
Protein Folding
Protein Structure, Tertiary
Grant Support
ID/Acronym/Agency:
GM080642/GM/NIGMS NIH HHS; R01 GM080642/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Anti-HIV Agents; 0/Carbohydrates; 0/Lectins; PHA4727WTP/Mannose
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  [Robert Schumann was born 200 years ago (1810-1856)].
Next Document:  Clustering of the neural cell adhesion molecule (NCAM) at the neuronal cell surface induces caspase-...