About: Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin

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About: Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin 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, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin
Creator	Wlodawer, Alexander Dwek, Raymond Mcmahon, James O'keefe, Barry Palmer, Kenneth Shenoy, Shilpa Zió Łkowska, Natasza Wormald, Mark
source	Medline; PMC
abstract	The mode of binding of oligosaccharides to griffithsin, an antiviral lectin from the red alga Griffithsia sp., was investigated by a combination of X‐ray crystallography, isothermal titration calorimetry, and molecular modeling. The structures of complexes of griffithsin with 1→6α‐mannobiose and with maltose were solved and refined at the resolution of 2.0 and 1.5 Å, respectively. The thermodynamic parameters of binding of 1→6α‐mannobiose, maltose, and mannose to griffithsin were determined. Binding profiles of 1→6α‐mannobiose and mannose were similar with K (d) values of 83.3 μM and 102 μM, respectively. The binding of maltose to griffithsin was significantly weaker, with a fourfold lower affinity (K (d) = 394 μM). In all cases the binding at 30°C was entropically rather than enthalpically driven. On the basis of the experimental crystal structures, as well as on previously determined structures of complexes with monosaccharides, it was possible to create a model of a tridentate complex of griffithsin with Man(9)GlcNAc(2), a high mannose oligosaccharide commonly found on the surface of viral glycoproteins. All shorter oligomannoses could be modeled only as bidentate or monodentate complexes with griffithsin. The ability to mediate tight multivalent and multisite interactions with high‐mannose oligosaccharides helps to explain the potent antiviral activity of griffithsin. Proteins 2007. © 2007 Wiley‐Liss, Inc.
has issue date	2007-03-05(xsd:dateTime)
bibo:doi	10.1002/prot.21336
bibo:pmid	17340634
has license	no-cc
sha1sum (hex)	965d61f25db80de4448adf519ac952272d6f71e2
schema:url	https://doi.org/10.1002/prot.21336
resource representing a document's title	Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin
has PubMed Central identifier	PMC7167611
has PubMed identifier	17340634
schema:publication	Proteins
resource representing a document's body	covid:965d61f25db80de4448adf519ac952272d6f71e2#body_text
is schema:about of	named entity 'PROTEINS' named entity 'MODELED' covid:arg/965d61f25db80de4448adf519ac952272d6f71e2 named entity 'thermodynamic parameters' named entity 'monosaccharides' named entity 'tridentate' named entity 'antiviral' named entity 'mannose' named entity 'glycoproteins' named entity 'monodentate' named entity 'mannose' named entity 'griffithsin' named entity 'maltose' named entity 'X-ray crystallography' named entity 'mannose' named entity 'Oligosaccharides' named entity 'Crystallographic' named entity 'Molecular Modeling' named entity 'mannose' named entity 'glucose' named entity 'GlcNAc' named entity 'monomer' named entity 'molecular replacement' named entity 'maltose' named entity 'high affinity' named entity 'C112' named entity 'conformational entropy' named entity 'protein' named entity 'griffithsin' named entity 'sugar' named entity 'molecule' named entity 'sugar' named entity 'monodentate' named entity 'lectin' named entity 'glycans' named entity 'griffithsin' named entity 'conformation' named entity 'precipitation' named entity 'oligosaccharide' named entity 'molecule' named entity 'PDB' named entity 'orders of magnitude' named entity 'maltose' named entity 'X-ray diffraction' named entity 'agglutinin' named entity 'diffracted' named entity 'simulated annealing' named entity 'amino acid analyzer' named entity 'glucopyranose' named entity '30 mM' named entity 'griffithsin' named entity 'mannose' named entity 'mannose' named entity 'binding site' named entity 'lectin' named entity 'electron density' named entity 'protein' named entity 'protein' named entity 'binding site' named entity 'mannose' named entity 'oligosaccharides' named entity 'Macromolecular Crystallography' named entity 'griffithsin' named entity 'GlcNAc' named entity 'glucose' named entity 'griffithsin' named entity 'binding sites' named entity 'molecule' named entity 'maltose' named entity 'multivalent' named entity 'mannose' named entity 'carbohydrates' named entity 'carbohydrate' named entity 'lectins'

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