About: Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine
Creator	Wlodawer, Alexander O'keefe, Barry Shenoy, Shilpa Zió Łkowska, Natasza
source	Medline; PMC
abstract	Crystal structures of complexes of an antiviral lectin griffithsin (GRFT) with glucose and N-acetylglucosamine were solved and refined at high resolution. In both complexes, all six monosaccharide-binding sites of GRFT were occupied and the mode of binding was similar to that of mannose. In our previous attempts to obtain a complex with N-acetylglucosamine by soaking, only a single site was occupied; thus, cocrystallization was clearly superior despite lower concentration of the ligand. Isothermal titration calorimetric experiments with N-acetylglucosamine, glucose, and mannose provided enthalpic evidence of distinct binding differences between the three monosaccharides. A comparison of the mode of binding of different monosaccharides is discussed in the context of the antiviral activity of GRFT, based on specific binding to high-mannose-containing complex carbohydrates found on viral envelopes.
has issue date	2007-07-01(xsd:dateTime)
bibo:doi	10.1110/ps.072889407
bibo:pmid	17567736
has license	green-oa
sha1sum (hex)	1c9c33874c16f533cb679ec3f636c7cd33d5b1a0
schema:url	https://doi.org/10.1110/ps.072889407
resource representing a document's title	Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine
has PubMed Central identifier	PMC2206701
has PubMed identifier	17567736
schema:publication	Protein Science
resource representing a document's body	covid:1c9c33874c16f533cb679ec3f636c7cd33d5b1a0#body_text
is schema:about of	named entity 'ligand' named entity 'Crystal structures' named entity 'PROTEIN ' named entity 'COMPLEXES' named entity 'LIGAND' named entity 'MODE' named entity 'ANTIVIRAL' named entity 'SINGLE SITE' covid:arg/1c9c33874c16f533cb679ec3f636c7cd33d5b1a0 named entity 'CONTAINING' named entity 'EVIDENCE OF' named entity 'SIMILAR' named entity 'MANNOSE' named entity 'COMPLEXES' named entity 'ANTIVIRAL ACTIVITY' named entity 'CONTEXT' named entity 'BASED' named entity 'DIFFERENT' named entity 'BINDING' named entity 'STRUCTURES' named entity 'CARBOHYDRATES' named entity 'DISTINCT' named entity 'GLUCOSE' named entity 'CRYSTAL' named entity 'MONOSACCHARIDES' named entity 'FOUND' named entity 'OUR' named entity 'VIRAL' named entity 'PROVIDED' named entity 'SOAKING' named entity 'OBTAIN' named entity 'HIGH' named entity 'ANTIVIRAL' named entity 'COMPARISON' named entity 'LOWER' named entity 'N-ACETYLGLUCOSAMINE' named entity 'COMPLEX' named entity 'HIGH RESOLUTION' named entity 'LECTIN' named entity 'PREVIOUS' named entity 'SPECIFIC' named entity 'EXPERIMENTS' named entity 'TITRATION' named entity 'GLUCOSE' named entity 'MONOSACCHARIDE' named entity 'CONCENTRATION OF' named entity 'COCRYSTALLIZATION' named entity 'BINDING SITES' named entity 'N-ACETYLGLUCOSAMINE' named entity 'STUDIES' named entity 'SUPERIOR' named entity 'activity' named entity 'single' named entity 'resolution' named entity 'high' named entity 'mode of binding' named entity 'lectin' named entity 'monosaccharides' named entity 'N-acetylglucosamine' named entity 'Isothermal' named entity 'mannose' named entity 'mannose' named entity 'enthalpic' named entity 'N-acetylglucosamine' named entity 'glucose' named entity 'glucose' named entity 'Crystallographic studies' named entity 'lectin' named entity 'PDB' named entity 'glucose' named entity 'glucose' named entity 'oligosaccharides' named entity 'mannose' named entity 'viral envelope' named entity 'Protein Data Bank' named entity 'carbohydrate' named entity 'N-acetylglucosamine' named entity 'molecule'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software